Home / Articles / Current advances in the X-ray crystallography of proteins

Current advances in the X-ray crystallography of proteins

Evgenii Mitrofanovich Popov 1
Evgenii Mitrofanovich Popov
1 Moscow State Correspondence Institute of Food Industry
10.1070/RC1995v064n12ABEH000194
Published 30 November 1994
Communication , Volume 64, Issue 12, 1064-1104
0
Share
Cite this
GOST
 | 
Cite this
GOST
Copy cite
Popov E. M. Current advances in the X-ray crystallography of proteins // Russian Chemical Reviews. 1995. Vol. 64. No. 12. pp. 1064-1104.
GOST all authors (up to 50)
Copy cite
Popov E. M. Current advances in the X-ray crystallography of proteins // Russian Chemical Reviews. 1995. Vol. 64. No. 12. pp. 1064-1104.
RIS
 | 
Cite this
RIS
Copy cite
TY - JOUR
DO - 10.1070/RC1995v064n12ABEH000194
UR - https://rcr.colab.ws/publications/10.1070/RC1995v064n12ABEH000194
TI - Current advances in the X-ray crystallography of proteins
T2 - Russian Chemical Reviews
AU - Popov, Evgenii Mitrofanovich
PY - 1995
DA - 1994/11/30
PB - ANO Editorial Board of the journal Uspekhi Khimii
SP - 1064-1104
IS - 12
VL - 64
ER -
BibTex
 | 
Cite this
BibTex (up to 50 authors)
Copy cite
@article{1995_Popov,
author = {Evgenii Mitrofanovich Popov},
title = {Current advances in the X-ray crystallography of proteins},
journal = {Russian Chemical Reviews},
year = {1995},
volume = {64},
publisher = {ANO Editorial Board of the journal Uspekhi Khimii},
month = {Nov},
url = {https://rcr.colab.ws/publications/10.1070/RC1995v064n12ABEH000194},
number = {12},
pages = {1064--1104},
doi = {10.1070/RC1995v064n12ABEH000194}
}
MLA
Cite this
MLA
Copy cite
Popov, Evgenii Mitrofanovich. “Current advances in the X-ray crystallography of proteins.” Russian Chemical Reviews, vol. 64, no. 12, Nov. 1995, pp. 1064-1104. https://rcr.colab.ws/publications/10.1070/RC1995v064n12ABEH000194.
Views / Visits / Downloads
31 / 31 / 12

Abstract

The present state and prospects for the development of the X-ray crystallography of globular proteins are analysed. The mechanisms of the functioning of membrane receptors, the immune proteins of T-lymphocytes, the histone octameric core of nucleosomes, DNA topoisomerase, the aspartate proteases of retroviruses, and the proteins of the actomyosin complex of skeletal muscles are examined on the basis of the three-dimensional structures of the protein molecules which have become known in recent years. It is shown that the results of the X-ray diffraction analysis of proteins has played a decisive role in the creation of an experimental basis and the development of the approaches necessary for the establishment of theoretical biology. A large proportion of the review is devoted to the advances in X-ray crystallography as regards the sources of radiation, the phase problem, and the experimental conditions. The use of synchrotron radiation and the abandonment of multiplet isomorphous substitution in the determination of phases not only significantly simplify the study of the molecular structures of proteins but permit an approach to securing information about the structures of protein intermediates which had previously been inaccessible. The bibliography includes 324 references.

References

1.
The Structure of Ribonuclease-S at 6 A Resolution
Wyckoff H.W., Hardman K.D., Allewell N.M., Inagami T., Tsernoglou D., Johnson L.N., Richards F.M.
Journal of Biological Chemistry , 1967
2.
Tertiary Structure of Ribonuclease
KARTHA G., BELLO J., HARKER D.
Nature , 1967
3.
Three-dimensional Structure of Tosyl-α-chymotrypsin
MATTHEWS B.W., SIGLER P.B., HENDERSON R., BLOW D.M.
Nature , 1967
4.
THE STRUCTURE OF CARBOXYPEPTIDASE A, VI. SOME RESULTS AT 2.0-Å RESOLUTION, AND THE COMPLEX WITH GLYCYL-TYROSINE AT 2.8-Å RESOLUTION
Reeke G.N., Hartsuck J.A., Ludwig M.L., Quiocho F.A., Steitz T.A., Lipscomb W.N.
Proceedings of the National Academy of Sciences of the United States of America , 1967
5.
5
A. A. Krasnovskii
Dokl. Akad. Nauk SSSR , 1953
6.
6
V. B. Evstigneev
Dokl. Akad. Nauk SSSR , 1953
8.
Solubilization of membranes by detergents.
Helenius A., Simons K.
Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes , 1975
10.
X-ray structure analysis of a membrane protein complex
Deisenhofer J., Epp O., Miki K., Huber R., Michel H.
Journal of Molecular Biology , 1984
11.
11
T. T. Bannister
Diss. Abstr. , 1959
12.
The structure of porin from Rhodobacter capsulatus at 1.8 Å resolution
Weiss M.S., Kreusch A., Schiltz E., Nestel U., Welte W., Weckesser J., Schulz G.E.
FEBS Letters , 1991
14.
Three-Dimensional Structures of the Ligand-Binding Domain of the Bacterial Aspartate Receptor with and Without a Ligand
Milburn M.V., Privé G.G., Milligan D.L., Scott W.G., Yeh J., Jancarik J., Koshland D.E., Kim S.
Science , 1991
18.
18
A. A. Krasnovskii
Dokl. Akad. Nauk SSSR , 1951
20.
Atherosclerosis: the eicosanoid connection
Makheja A.
Molecular and Cellular Biochemistry , 1992
23.
Intracellular protein topogenesis
Blobel G.
Proceedings of the National Academy of Sciences of the United States of America , 1980
24.
24
M. S. Ashkinazi
Dokl. Akad. Nauk SSSR , 1951
25.
25
G. W. Robinson
J. Chem. Phys. , 1955
26.
26
B. Ya. Dain
1957
27.
The Biologic Roles of CD2, CD4, and CD8 in T-Cell Activation
Bierer B.E., Sleckman B.P., Ratnofsky S.E., Burakoff S.J.
Annual Review of Immunology , 1989
28.
28
A. A. Krasnovskii
Dokl. Akad. Nauk SSSR , 1955
30.
30
V. B. Evstigneev
Dokl. Akad. Nauk SSSR , 1954
31.
31
A. A. Krasnovskii
Biokhimiya , 1960
33.
33
M. B. Neiman
"Issledovanie Mekhanizma Okisleniya Butana" (Research on the Mechanism of the Oxidation of Butane) , 1939
35.
CD8 is required during positive selection of CD4-/CD8+ T cells.
Zúñiga-Pflücker J.C., Jones L.A., Longo D.L., Kruisbeek A.M.
Journal of Experimental Medicine , 1990
36.
CD8 is needed for development of cytotoxic T but not helper T cells
Fung-Leung W., Schilham M.W., Rahemtulla A., Kündig T.M., Vollenweider M., Potter J., van Ewijk W., Mak T.W.
Cell , 1991
38.
Transfection of the CD8 gene enhances T-cell recognition
Dembić Z., Haas W., Zamoyska R., Parnes J., Steinmetz M., von Boehmer H.
Nature , 1987
39.
Reconstitution of MHC class I specificity by transfer of the T cell receptor and Lyt-2 genes
Gabert J., Langlet C., Zamoyska R., Parnes J.R., Schmitt-Verhulst A., Malissen B.
Cell , 1987
41.
Direct evidence for binding of CD8 to HLA class I antigens.
Rosenstein Y., Ratnofsky S., Burakoff S.J., Herrmann S.H.
Journal of Experimental Medicine , 1989
42.
A binding site for the T-cell co-receptor CD8 on the α3 domain of HLA-A2
Salter R.D., Benjamin R.J., Wesley P.K., Buxton S.E., Garrett T.P., Clayberger C., Krensky A.M., Norment A.M., Littman D.R., Parham P.
Nature , 1990
43.
Mutations in CD8 that affect interactions with HLA class I and monoclonal anti-CD8 antibodies.
Sanders S.K., Fox R.O., Kavathas P.
Journal of Experimental Medicine , 1991
47.
Structure of the human class I histocompatibility antigen, HLA-A2
Bjorkman P.J., Saper M.A., Samraoui B., Bennett W.S., Strominger J.L., Wiley D.C.
Nature , 1987
48.
A hypothetical model of the foreign antigen binding site of Class II histocompatibility molecules
Brown J.H., Jardetzky T., Saper M.A., Samraoui B., Bjorkman P.J., Wiley D.C.
Nature , 1988
49.
Crystal structure of an extracellular fragment of the rat CD4 receptor containing domains 3 and 4
Lange G., Lewis S.J., Murshudov G.N., Dodson G.G., Moody P.C., Turkenburg J.P., Barclay A.N., Brady R.L.
Structure , 1994
50.
Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains
Wang J., Yan Y., Garrett T.P., Liu J., Rodgers D.W., Garlick R.L., Tarr G.E., Husain Y., Reinherz E.L., Harrison S.C.
Nature , 1990
51.
Refinement and Analysis of the Structure of the First Two Domains of Human CD4
Garrett T.P., Wang J., Yan Y., Liu J., Harrison S.C.
Journal of Molecular Biology , 1993
52.
Crystal Structure of Domains 3 and 4 of Rat CD4: Relation to the NH 2 -Terminal Domains
Brady R.L., Dodson E.J., Dodson G.G., Lange G., Davis S.J., Williams A.F., Barclay A.N.
Science , 1993
53.
Identification of a CD4 binding site on the β2 domain of HLA-DR molecules
Cammarota G., Scheirle A., Takacs B., Doran D.M., Knorr R., Bannwarth W., Guardiola J., Sinigaglia F.
Nature , 1992
56.
Designing CD4 immunoadhesins for AIDS therapy
Capon D.J., Chamow S.M., Mordenti J., Marsters S.A., Gregory T., Mitsuya H., Byrn R.A., Lucas C., Wurm F.M., Groopman J.E., Broder S., Smith D.H.
Nature , 1989
57.
T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV
Klatzmann D., Champagne E., Chamaret S., Gruest J., Guetard D., Hercend T., Gluckman J., Montagnier L.
Nature , 1984
58.
The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus
Dalgleish A.G., Beverley P.C., Clapham P.R., Crawford D.H., Greaves M.F., Weiss R.A.
Nature , 1984
59.
Structural Diversity in Domains of the Immunoglobulin Superfamily
Williams A.F., Davis S.J., He Q., Barclay A.N.
Cold Spring Harbor Symposia on Quantitative Biology , 1989
60.
Molecular characteristics of recombinant human CD4 as deduced from polymorphic crystals.
Kwong P.D., Ryu S.E., Hendrickson W.A., Axel R., Sweet R.M., Folena-Wasserman G., Hensley P., Sweet R.W.
Proceedings of the National Academy of Sciences of the United States of America , 1990
61.
High level expression in Chinese hamster ovary cells of soluble forms of CD4 T lymphocyte glycoprotein including glycosylation variants.
Davis S.J., Ward H.A., Puklavec M.J., Willis A.C., Williams A.F., Barclay A.N.
Journal of Biological Chemistry , 1990
62.
Peptides Presented to the Immune System by the Murine Class II Major Histocompatibility Complex Molecule I-A d
Hunt D.F., Michel H., Dickinson T.A., Shabanowitz J., Cox A.L., Sakaguchi K., Appella E., Grey H.M., Sette A.
Science , 1992
63.
Specificity and promiscuity among naturally processed peptides bound to HLA-DR alleles.
Chicz R.M., Urban R.G., Gorga J.C., Vignali D.A., Lane W.S., Strominger J.L.
Journal of Experimental Medicine , 1993
64.
Tiwari J.L., Terasaki P.I.
1985
65.
A Molecular Basis for MHC Class II—Associated Autoimmunity
Todd J.A., Acha-Orbea H., Bell J.I., Chao N., Fronek Z., Jacob C.O., McDermott M., Sinha A.A., Timmerman L., Steinman L., McDevitt H.O.
Science , 1988
66.
Crystallization of HLA-DR antigens
Gorga J.C., Brown J.H., Jardetzky T., Wiley D.C., Strominger J.L.
Research in Immunology , 1991
67.
Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1
Brown J.H., Jardetzky T.S., Gorga J.C., Stern L.J., Urban R.G., Strominger J.L., Wiley D.C.
Nature , 1993
69.
Molecular Components of T-Cell Recognition
Jorgensen J.L., Reay P.A., Ehrich E.W., Davis M.M.
Annual Review of Immunology , 1992
71.
Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
Falk K., Rötzschke O., Stevanovié S., Jung G., Rammensee H.
Nature , 1991
72.
Characterization of Peptides Bound to the Class I MHC Molecule HLA-A2.1 by Mass Spectrometry
Hunt D.F., Henderson R.A., Shabanowitz J., Sakaguchi K., Michel H., Sevilir N., Cox A.L., Appella E., Engelhard V.H.
Science , 1992
73.
Identification of self peptides bound to purified HLA-B27
Jardetzky T.S., Lane W.S., Robinson R.A., Madden D.R., Wiley D.C.
Nature , 1991
74.
Truncation variants of peptides isolated from MHC class II molecules suggest sequence motifs
Rudensky A.Y., Preston-Hurlburt, P., Al-Ramadi B.K., Rothbard J., Janeway C.A.
Nature , 1992
75.
Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size
Chicz R.M., Urban R.G., Lane W.S., Gorga J.C., Stern L.J., Vignali D.A., Strominger J.L.
Nature , 1992
76.
Promiscuous and allele-specific anchors in HLA-DR-binding peptides
Hammer J., Valsasnini P., Tolba K., Bolin D., Higelin J., Takacs B., Sinigaglia F.
Cell , 1993
77.
HLA DR4w4-binding motifs illustrate the biochemical basis of degeneracy and specificity in peptide-DR interactions.
Sette A., Sidney J., Oseroff C., del Guercio M.F., Southwood S., Arrhenius T., Powell M.F., Colón S.M., Gaeta F.C., Grey H.M.
Journal of Immunology , 1993
78.
The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation
Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C.
Nature , 1991
80.
Atomic structure of a human MHC molecule presenting an influenza virus peptide
Silver M.L., Guo H., Strominger J.L., Wiley D.C.
Nature , 1992
82.
Crystal structure of the major histocompatibility complex class I H-2Kb molecule containing a single viral peptide: implications for peptide binding and T-cell receptor recognition.
Zhang W., Young A.C., Imarai M., Nathenson S.G., Sacchettini J.C.
Proceedings of the National Academy of Sciences of the United States of America , 1992
84.
Crystal Structures of Two Viral Peptides in Complex with Murine MHC Class I H-2K b
Fremont D.H., Matsumura M., Stura E.A., Peterson P.A., Wilson L.A.
Science , 1992
85.
Peptide binding to the major histocompatibility complex molecules
Madden D.R., Wiley D.C.
Current Opinion in Structural Biology , 1992
86.
Emerging Principles for the Recognition of Peptide Antigens by MHC Class I Molecules
Matsumura M., Fremont D.H., Peterson P.A., Wilson L.A.
Science , 1992
87.
Comparison of the P2 specificity pocket in three human histocompatibility antigens: HLA-A*6801, HLA-A*0201, and HLA-B*2705.
Guo H.C., Madden D.R., Silver M.L., Jardetzky T.S., Gorga J.C., Strominger J.L., Wiley D.C.
Proceedings of the National Academy of Sciences of the United States of America , 1993
88.
Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
Stern L.J., Brown J.H., Jardetzky T.S., Gorga J.C., Urban R.G., Strominger J.L., Wiley D.C.
Nature , 1994
89.
X-Ray Crystallographic Studies of Pepsin
Andreeva N.S., Gustchina A.E., Fedorov A.A., Shutzkever N.E., Volnova T.V.
Advances in Experimental Medicine and Biology , 1977
90.
95
A. A. Krasnovskii
Fiziologiya Rastenii , 1957
91.
96
L. M. Vorob'eva
Biokhimiya , 1958
92.
Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution.
Sielecki A.R., Fedorov A.A., Boodhoo A., Andreeva N.S., James M.N.
Journal of Molecular Biology , 1990
96.
101
M. F. Shostakovskii
Izv. Akad. Nauk SSSR, Otd. Khim. Nauk , 1960
97.
102
F. Fichter
Helv. Chim. Acta , 1922
98.
103
L. N. Bell
Dokl. Akad. Nauk SSSR , 1956
99.
The three‐dimensional structure of recombinant bovine chymosin at 2.3 Å resolution
Gilliland G.L., Winborne E.L., Nachman J., Wlodawer A.
Proteins: Structure, Function and Genetics , 1990
100.
Structure of Recombinant Human Renin, a Target for Cardiovascular-Active Drugs, at 2.5 Å Resolution
Sielecki A.R., Hayakawa K., Fujinaga M., Murphy M.E., Fraser M., Muir A.K., Carilli C.T., Lewicki J.A., Baxter J.D., James M.N.
Science , 1989
102.
X-ray analyses of peptide–inhibitor complexes define the structural basis of specificity for human and mouse renins
Dhanaraj V., Dealwis C.G., Frazao C., Badasso M., Sibanda B.L., Tickle I.J., Cooper J.B., Driessen H.P., Newman M., Aguilar C., Wood S.P., Blundell T.L., Hobart P.M., Geoghegan K.F., Ammirati M.J., et. al.
Nature , 1992
103.
X-ray analysis at 2.0 A resolution of mouse submaxillary renin complexed with a decapeptide inhibitor CH-66, based on the 4-16 fragment of rat angiotensinogen.
Dealwis C.G., Frazao C., Badasso M., Cooper J.B., Tickle I.J., Driessen H., Blundell T.L., Murakami K., Miyazaki H., Sueiras-Diaz J., Jones D.M., Szelke M.
Journal of Molecular Biology , 1994
104.
Comparative enzymatic studies of human renin acting on pure natural or synthetic substrates
Cumin F., Le-Nguyen D., Castro B., Menard J., Corvol P.
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology , 1987
106.
Structure and refinement of penicillopepsin at 1.8 A resolution.
James M.N., Sielecki A.R.
Journal of Molecular Biology , 1983
108.
Conformational flexibility in the active sites of aspartyl proteinases revealed by a pepstatin fragment binding to penicillopepsin.
James M.N., Sielecki A., Salituro F., Rich D.H., Hofmann T.
Proceedings of the National Academy of Sciences of the United States of America , 1982
110.
Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica.
Subramanian E., Swan I.D., Liu M., Davies D.R., Jenkins J.A., Tickle I.J., Blundell T.L.
Proceedings of the National Academy of Sciences of the United States of America , 1977
112.
X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.
Blundell T.L., Jenkins J.A., Sewell B.T., Pearl L.H., Cooper J.B., Tickle I.J., Veerapandian B., Wood S.P.
Journal of Molecular Biology , 1990
113.
The structure of a synthetic pepsin inhibitor complexed with endothiapepsin.
COOPER J., FOUNDLING S., HEMMINGS A., BLUNDELL T., JONES D.M., HALLETT A., SZELKE M.
FEBS Journal , 1987
115.
X-ray studies of aspartic proteinase-statine inhibitor complexes
Cooper J.B., Foundling S.I., Blundell T.L., Boger J., Jupp R.A., Kay J.
Biochemistry , 1989
116.
The Crystal Structure of an Acid Protease from Rhizopus Chinensis at 2.5 a Resolution
Subramanian E., Liu M., Swan I.D., Davies D.R.
Advances in Experimental Medicine and Biology , 1977
117.
Structure and refinement at 1.8 A resolution of the aspartic proteinase from Rhizopus chinensis.
Suguna K., Bott R.R., Padlan E.A., Subramanian E., Sheriff S., Cohen G.H., David D.
Journal of Molecular Biology , 1987
119.
Binding of a reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: implications for a mechanism of action.
Suguna K., Padlan E.A., Smith C.W., Carlson W.D., Davies D.R.
Proceedings of the National Academy of Sciences of the United States of America , 1987
120.
125
K. A. Andrianov
Vysokomol. Soed. , 1960
121.
Crystal structure of a retroviral protease proves relationship to aspartic protease family
Miller M., Jaskólski M., Rao J.K., Leis J., Wlodawer A.
Nature , 1989
122.
Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1
Navia M.A., Fitzgerald P.M., McKeever B.M., Leu C., Heimbach J.C., Herber W.K., Sigal I.S., Darke P.L., Springer J.P.
Nature , 1989
123.
Conserved Folding in Retroviral Proteases: Crystal Structure of Synthetic HIV-1 Protease
Wlodawer A., Miller M., Jaskólski M., Sathyanarayana B.K., Baldwin E., Weber I.T., Selk L.M., Clawson L., Schneider J., Kent S.B.
Science , 1989
124.
Structure at 2.5-.ANG. resolution of chemically synthesized Human Immunodeficiency Virus Type 1 protease complexed with a hydroxyethylene-based inhibitor
Jaskolski M., Tomasselli A.G., Sawyer T.K., Staples D.G., Heinrikson R.L., Schneider J., Kent S.B., Wlodawer A.
Biochemistry , 1991
125.
X-ray crystallographic structure of a complex between a synthetic protease of human immunodeficiency virus 1 and a substrate-based hydroxyethylamine inhibitor.
Swain A.L., Miller M.M., Green J., Rich D.H., Schneider J., Kent S.B., Wlodawer A.
Proceedings of the National Academy of Sciences of the United States of America , 1990
126.
Structure of Complex of Synthetic HIV-1 Protease with a Substrate-Based Inhibitor at 2.3 Å Resolution
Miller M., Schneider J., Sathyanarayana B.K., Toth M.V., Marshall G.R., Clawson L., Selk L., Kent S.B., Wlodawer A.
Science , 1989
127.
Crystal structure of a tethered dimer of HIV-1 proteinase complexed with an inhibitor
Bhat T.N., Baldwin E.T., Liu B., Cheng Y.E., Erickson J.W.
Nature Structural Biology , 1994
128.
Domain flexibility in aspartic proteinases
Šali A., Veerapandian B., Cooper J.B., Moss D.S., Hofmann T., Blundell T.L.
Proteins: Structure, Function and Genetics , 1992
129.
Studies on the Mechanisms of Action of Proteolytic Enzymes Using Heavy Oxygen Exchange
ANTONOV V.K., GINODMAN L.M., RUMSH L.D., KAPITANNIKOV Y.V., BARSHEVSKAYA T.N., YAVASHEV L.P., GUROVA A.G., VOLKOVA L.I.
FEBS Journal , 2005
130.
New Data on Pepsin Mechanism and Specificity
Antonov V.K.
Advances in Experimental Medicine and Biology , 1977
131.
Mechanism of pepsin catalysis: General base catalysis by the active‐site carboxylate ion
Antonov V.K., Ginodman L.M., Kapitannikov Y.V., Barshevskaya T.N., Gurova A.G., Rumsh L.D.
FEBS Letters , 1978
132.
137
S. R. Rafikov
Zh. Obshch. Khim. , 1944
133.
138
S. Ono
J. Chem. Soc. Japan , 1957
134.
Molecular Targets for AIDS Therapy
Mitsuya H., Yarchoan R., Broder S.
Science , 1990
135.
140
1912
136.
Active human immunodeficiency virus protease is required for viral infectivity.
Kohl N.E., Emini E.A., Schleif W.A., Davis L.J., Heimbach J.C., Dixon R.A., Scolnick E.M., Sigal I.S.
Proceedings of the National Academy of Sciences of the United States of America , 1988
137.
HIV protease: a novel chemotherapeutic target for AIDS
Huff J.R.
Journal of Medicinal Chemistry , 1991
138.
A structural model for the retroviral proteases
Pearl L.H., Taylor W.R.
Nature , 1987
139.
Stability and activity of human immunodeficiency virus protease: comparison of the natural dimer with a homologous, single-chain tethered dimer.
Cheng Y.S., Yin F.H., Foundling S., Blomstrom D., Kettner C.A.
Proceedings of the National Academy of Sciences of the United States of America , 1990
140.
Characterization of an active single polypeptide form of the human immunodeficiency virus type 1 protease.
DiIanni C.L., Davis L.J., Holloway M.K., Herber W.K., Darke P.L., Kohl N.E., Dixon R.A.
Journal of Biological Chemistry , 1990
141.
Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A.
Seelmeier S., Schmidt H., Turk V., von der Helm K.
Proceedings of the National Academy of Sciences of the United States of America , 1988
143.
Complete mutagenesis of the HIV-1 protease
Loeb D.D., Swanstrom R., Everitt L., Manchester M., Stamper S.E., Hutchison C.A.
Nature , 1989
145.
Inhibition of HIV protease activity by heterodimer formation
Babe L.M., Pichuantes S., Craik C.S.
Biochemistry , 1991
146.
Three-dimensional structure of β-galactosidase from E. coli.
Jacobson R.H., Zhang X.-., DuBose R.F., Matthews B.W.
Nature , 1994
147.
Inactivation of pepsin by diphenyldiazomethane.
Delpierre G.R., Fruton J.S.
Proceedings of the National Academy of Sciences of the United States of America , 1965
148.
154
Friedl.
150.
156
J. S. Fruton
J. Biol. Med. , 1950
151.
157
1903
152.
158
Friedl.
153.
159
J. Tafel
Z. Elektrochem. , 1911
155.
161
Friedl.
156.
162
1917
157.
163
Friedl.
159.
An octamer of histones in chromatin and free in solution.
Thomas J.O., Kornberg R.D.
Proceedings of the National Academy of Sciences of the United States of America , 1975
161.
A low resolution structure for the histone core of the nucleosome
Klug A., Rhodes D., Smith J., Finch J.T., Thomas J.O.
Nature , 1980
164.
Histones
Isenberg I.
Annual Review of Biochemistry , 1979
165.
The subunit structure of the eukaryotic chromosome
Baldwin J.P., Boseley P.G., Bradbury E.M., Ibel K.
Nature , 1975
167.
Crystal structure of the nucleosome core particle at 16 Å resolution
Bentley G.A., Lewit-Bentley A., Finch J.T., Podjarny A.D., Roth M.
Journal of Molecular Biology , 1984
168.
Structure of nucleosome core particles of chromatin
Finch J.T., Lutter L.C., Rhodes D., Brown R.S., Rushton B., Levitt M., Klug A.
Nature , 1977
169.
X-ray diffraction study of a new crystal form of the nucleosome core showing higher resolution
Finch J.T., Brown R.S., Rhodes D., Richmond T., Rushton B., Lutter L.C., Klug A.
Journal of Molecular Biology , 1981
170.
Structure of the nucleosome core particle at 7 Å resolution
Richmond T.J., Finch J.T., Rushton B., Rhodes D., Klug A.
Nature , 1984
171.
Crystals of the Octameric Histone Core of the Nucleosome
Burlingame R.W., Love W.E., Moudrianakis E.N.
Science , 1984
172.
Crystallographic Structure of the Octameric Histone Core of the Nucleosome at a Resolution of 3.3 Å
Burlingame R.W., Love W.E., Wang B., Hamlin R., Xuong N., Moudrianakis E.N.
Science , 1985
173.
The Octameric Histone Core of the Nucleosome
Wang B., Rose J., Arents G., Moudrianakis E.N.
Journal of Molecular Biology , 1994
174.
180
1946
177.
A hyper-recombination mutation in S. cerevisiae identifies a novel eukaryotic topoisomerase
Wallis J.W., Chrebet G., Brodsky G., Rolfe M., Rothstein R.
Cell , 1989
180.
Reverse gyrase: a helicase-like domain and a type I topoisomerase in the same polypeptide.
Confalonieri F., Elie C., Nadal M., de La Tour C., Forterre P., Duguet M.
Proceedings of the National Academy of Sciences of the United States of America , 1993
181.
187
1954
185.
Wang J.C.
Scientific American , 1982
186.
Crystallization of a 67 kDa Fragment of Escherichia coli DNA Topoisomerase I
Lima C.D., Wang J.C., Mondragón A.
Journal of Molecular Biology , 1993
187.
Schulz G.E., Schirmer R.H.
1979
188.
194
A. A. Vertman
"Svoistva Rasplavov Zheleza" (Properties of Iron Melts) , 1969
189.
195
M. Allen
J. Chem. Soc. , 1961
190.
196
E. Müller
Z. Elektrochem. , 1910
194.
Electron microscope studies of the organisation of the filaments in striated muscle
Huxley H.E.
Biochimica et Biophysica Acta - General Subjects , 1953
196.
Myosine and Adenosinetriphosphatase
ENGELHARDT W.A., LJUBIMOWA M.N.
Nature , 1939
197.
204
Cherkesov A I
Ref. Zh. Khim. , 1968
199.
206
J. Petersen
Z. Phys. Chem. , 1900
201.
Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy.
Henderson R., Baldwin J.M., Ceska T.A., Zemlin F., Beckmann E., Downing K.H.
Journal of Molecular Biology , 1990
202.
Atomic model of plant light-harvesting complex by electron crystallography
Kühlbrandt W., Wang D.N., Fujiyoshi Y.
Nature , 1994
207.
Atomic model of the actin filament
Holmes K.C., Popp D., Gebhard W., Kabsch W.
Nature , 1990
208.
Atomic structure of the actin: DNase I complex
Kabsch W., Mannherz H.G., Suck D., Pai E.F., Holmes K.C.
Nature , 1990
210.
217
1925
211.
Crystallographic R Factor Refinement by Molecular Dynamics
Brünger A.T., Kuriyan J., Karplus M.
Science , 1987
212.
A Comparison of the Atomic Model of F-Actin with Cryo-Electron Micrographs of Actin and Decorated Actin
Holmes K.C., Tirion M., Popp D., Lorenz M., Kabsch W., Milligan R.A.
Advances in Experimental Medicine and Biology , 1993
213.
Molecular structure of F-actin and location of surface binding sites
Milligan R.A., Whittaker M., Safer D.
Nature , 1990
214.
Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation.
Lowey S., Slayter H.S., Weeds A.G., Baker H.
Journal of Molecular Biology , 1969
215.
Substructure of the myosin molecule. II. The light chains of myosin.
Weeds A.G., Lowey S.
Journal of Molecular Biology , 1971
216.
Homogeneity of myosin subfragments by equilibrium centrifugation
Margossian S.S., Stafford W.F., Lowey S.
Biochemistry , 1981
218.
225
1960
219.
The degradation of heavy meromyosin by trypsin
MUELLER H., PERRY S.
Biochemical Journal , 1962
221.
Regulation of non-muscle myosin structure and function
Citi S., Kendrick-Jones J.
BioEssays , 1987
222.
Regulation of cytoplasmic and smooth muscle myosin.
Sellers J.R.
Current Opinion in Cell Biology , 1991
223.
Shape and flexibility of the myosin molecule.
Elliott A., Offer G.
Journal of Molecular Biology , 1978
224.
Packing analysis of crystalline myosin subfragment-1
Winkelmann D.A., Mekeel H., Rayment I.
Journal of Molecular Biology , 1985
226.
Three-dimensional structure of myosin subfragment-1: a molecular motor
Rayment I., Rypniewski W., Schmidt-Base K., Smith R., Tomchick D., Benning M., Winkelmann D., Wesenberg G., Holden H.
Science , 1993
228.
235
R. Peffen
1967
229.
Structure of the actin-myosin complex and its implications for muscle contraction
Rayment I., Holden H., Whittaker M., Yohn C., Lorenz M., Holmes K., Milligan R.
Science , 1993
230.
Electron microscopy of scallop myosin. Location of regulatory light chains.
Flicker P.F., Wallimann T., Vibert P.
Journal of Molecular Biology , 1983
231.
Photochemical mapping of the active site of myosin
Yount R G, Cremo C R, Grammer J C, Kerwin B A
Philosophical Transactions of the Royal Society B: Biological Sciences , 1992
236.
Mechanism of actomyosin ATPase and the problem of muscle contraction.
Taylor E.W., Trenlham D.R.
CRC Critical Reviews in Biochemistry , 1979
237.
RELATIONSHIPS BETWEEN CHEMICAL AND MECHANICAL EVENTS DURING MUSCULAR CONTRACTION
Hibberd M.G., Trentham D.R.
Annual Review of Biophysics and Bioengineering , 1986
238.
Small-Angle Synchrotron X-Ray Scattering Reveals Distinct Shape Changes of the Myosin Head During Hydrolysis of ATP
Wakabayashi K., Tokunaga M., Kohno I., Sugimoto Y., Hamanaka T., Takezawa Y., Wakabayashi T., Amemiya Y.
Science , 1992
240.
How molecular motors work
Spudich J.A.
Nature , 1994
242.
Single myosin molecule mechanics: piconewton forces and nanometre steps
Finer J.T., Simmons R.M., Spudich J.A.
Nature , 1994
243.
Use of Synchrotron Orbit‐Radiation in X‐Ray Physics
Parratt L.G.
Review of Scientific Instruments , 1959
244.
Synchrotron radiation as a light source
Godwin R.P.
Springer Tracts in Modern Physics , 1969
245.
Synchrotron Radiation as a Source for X-ray Diffraction
ROSENBAUM G., HOLMES K.C., WITZ J.
Nature , 1971
246.
253
D. Goerrig
Chem. Abs. , 1959
247.
254
M. G. Safarov
1975
248.
255
Tomita M
Chem. Abs. , 1939
249.
256
Z. V. Zvonkova
Zh. Strukt. Khim. , 1977
250.
Applications of synchrotron radiation to protein crystallography: preliminary results.
Phillips J.C., Wlodawer A., Yevitz M.M., Hodgson K.O.
Proceedings of the National Academy of Sciences of the United States of America , 1976
252.
259
V. Elyutin
Trudy Moskov. Inst. Stali , 1939
253.
Laue diffraction study on the structure of cytochrome c peroxidase compound I.
Fülöp V., Phizackerley R.P., Soltis S.M., Clifton I.J., Wakatsuki S., Erman J., Hajdu J., Edwards S.L.
Structure , 1994
254.
Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution.
Nikkola M., Lindqvist Y., Schneider G.
Journal of Molecular Biology , 1994
255.
The Hydrolytic Water Molecule in Trypsin, Revealed by Time-Resolved Laue Crystallography
Singer P.T., Smalås A., Carty R.P., Mangel W.F., Sweet R.M.
Science , 1993
256.
The crystal structure of glucose dehydrogenase from Thermoplasma acidophilum
John J., Crennell S.J., Hough D.W., Danson M.J., Taylor G.L.
Structure , 1994
257.
Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase
Verschueren K.H., Seljée F., Rozeboom H.J., Kalk K.H., Dijkstra B.W.
Nature , 1993
258.
The crystal structure of affinity-matured human growth hormone at 2 A resolution.
Ultsch M.H., Somers W., Kossiakoff A.A., de Vos A.M.
Journal of Molecular Biology , 1994
259.
Crystal structures of aconitase with trans-aconitate and nitrocitrate bound.
Lauble H., Kennedy M.C., Beinert H., Stout C.D.
Journal of Molecular Biology , 1994
260.
The Refined Structures of a Stabilized Mutant and of Wild-type Pyruvate Oxidase from Lactobacillus plantarum
Muller Y.A., Schumacher G., Rudolph R., Schulz G.E.
Journal of Molecular Biology , 1994
261.
Atomic resolution (0.83 A) crystal structure of the hydrophobic protein crambin at 130 K.
Teeter M.M., Roe S.M., Heo N.H.
Journal of Molecular Biology , 1993
262.
Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 A resolution.
Housset D., Habersetzer-Rochat C., Astier J., Fontecilla-Camps J.C.
Journal of Molecular Biology , 1994
263.
Refinement of recombinant oncomodulin at 1.30 A resolution.
Ahmed F.R., Rose D.R., Evans S.V., Pippy M.E., To R.
Journal of Molecular Biology , 1993
265.
Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
Ramakrishnan V., Finch J.T., Graziano V., Lee P.L., Sweet R.M.
Nature , 1993
266.
Structure of restriction endonuclease BamHI phased at 1.95 å resolution by MAD analysis
Newman M., Strzelecka T., Dorner L., Schildkraut I., Aggarwal A.
Structure , 1994
267.
276
St. C. H. Deville
Ann. Chim. Phys. , 1859
268.
Structure of the Allosteric Regulatory Enzyme of Purine Biosynthesis
Smith J.L., Zaluzec E.J., Wery J., Niu L., Switzer R.L., Zalkin H., Satow Y.
Science , 1994
269.
Architecture of the invisible
Thomas J.M.
Nature , 1993
270.
Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes.
Franken S.M., Rozeboom H.J., Kalk K.H., Dijkstra B.W.
EMBO Journal , 1991
271.
280
B. de Jassonneix
Compt. rend. , 1906
272.
281
B. de Jassonneix
Compt. rend. , 1906
273.
282
B. de Jassonneix
Compt. rend. , 1906
274.
283
H. Moissan
Compt. rend. , 1902
275.
284
H. Moissan
Compt. rend. , 1902
279.
Structural basis of the activation and action of trypsin
Huber R., Bode W.
Accounts of Chemical Research , 1978
282.
Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor
Rühlmann A., Kukla D., Schwager P., Bartels K., Huber R.
Journal of Molecular Biology , 1973
283.
Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor
Huber R., Kukla D., Bode W., Schwager P., Bartels K., Deisenhofer J., Steigemann W.
Journal of Molecular Biology , 1974
286.
Mössbauer spectroscopic study of compound es of cytochrome c peroxidase
Lang G., Spartalian K., Yonetani T.
Biochimica et Biophysica Acta - General Subjects , 1976
288.
Crystal structure of cytochrome c peroxidase compound I
Edwards S.L., Nguyen Huu Xuong, Hamlin R.C., Kraut J.
Biochemistry , 1987
290.
Crystal structure of photolysed carbonmonoxy-myoglobin
Schlichting I., Berendzen J., Phillips G.N., Sweet R.M.
Nature , 1994
291.
Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K
Teng T.-., Šrajer V., Moffat K.
Nature Structural and Molecular Biology , 1994
292.
The little Big Bang
Petsko G.A.
Nature , 1994
296.
305
T. Yano
1968
297.
Nonexponential relaxation after ligand dissociation from myoglobin: a molecular dynamics simulation.
Kuczera K., Lambry J.C., Martin J.L., Karplus M.
Proceedings of the National Academy of Sciences of the United States of America , 1993
298.
307
Y. Doi
Chem. Abs. , 1968
299.
The structure of haemoglobin - IV. Sign determination by the isomorphous replacement method
Proceedings of the Royal Society A: Mathematical, Physical and Engineering Sciences , 1954
300.
Zur Dispersionstheorie der R�ntgenstrahlen
H�nl H.
European Physical Journal A , 1933
301.
310
R. Paris
Chimie et Industrie , 1969
302.
311
L. A. Dvorina
Zh. Prikl. Khim. , 1968
304.
Crystal structure study ofOpsanus tauparvalbumin by multiwavelength anomalous diffraction
Kahn R., Fourme R., Bosshard R., Chiadmi M., Risler J.L., Dideberg O., Wery J.P.
FEBS Letters , 1985
305.
Crystal structure analysis of cytochrome c' by the multiwavelength anomalous diffraction method using synchrotron radiation
Harada S., Yasui M., Murakawa K., Kasai N., Satow Y.
Journal of Applied Crystallography , 1986
307.
Measurement and use of anomalous X-ray scattering
Hendrickson W.A.
Acta Crystallographica Section A Foundations of Crystallography , 1984
308.
Multiple-wavelength phase determination in protein crystallography
Smith J.L., Pähler A., Krishna Murthy H.M., Hendrickson W.A.
Acta Crystallographica Section A Foundations of Crystallography , 1987
309.
318
1968
310.
Crystallographic structure analysis of lamprey hemoglobin from anomalous dispersion of synchrotron radiation
Hendrickson W.A., Smith J.L., Phizackerley R.P., Merritt E.A.
Proteins: Structure, Function and Genetics , 1988
312.
Biosynthesis by Escherichia coli of active altered proteins containing selenium instead of sulfur.
Cowie D.B., Cohen G.N.
Biochimica et Biophysica Acta - General Subjects , 1957
315.
324
H. A. Ohlgren
1969
316.
325
G. A. Meerson
Neorg. Materialy , 1970