Zobrazeno 1 - 10
of 14
pro vyhledávání: '"B V, Strokopytov"'
Publikováno v:
Journal of Applied Crystallography. 31:98-102
The BLANC program suite is a set of programs which can be used for macromolecular structure determination by X-ray crystallography. The suite is designed to provide experienced crystallographers and students with a number of simple tools, at the same
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fc8610ebb3616d47109145654eea6daf
https://doi.org/10.1107/s0021889897007796
https://doi.org/10.1107/s0021889897007796
Autor:
Zbigniew Dauter, Keith S. Wilson, B. V. Strokopytov, Yurii M. Torchinsky, V.V. Borisov, Vladimir N. Malashkevich
Publikováno v:
Journal of Molecular Biology. 247:111-124
The crystal structure of chicken cytosolic aspartate aminotransferase (cAATase; EC 2.6.1.1) has been solved and refined at 1.9 A resolution. Orthorhombic crystals, space group P2(1)2(1)2(1), a = 56.4 A, b = 126.0 A and c = 142.3 A, were grown from po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afa11dfa260901debe07583a0812009a
https://doi.org/10.1006/jmbi.1994.0126
https://doi.org/10.1006/jmbi.1994.0126
Autor:
Michael Matz, Kostya Polyakov, Sergei Smulevitch, Olga V. Galperina, Andrei L. Osterman, Olga Zagnitko, Valentin M. Stepanov, Nikolai V. Grishin, B. V. Strokopytov, G. Obmolova, Alexei Teplyakov, Inna P. Kuranova
Publikováno v:
European Journal of Biochemistry. 208:281-288
The crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris has been determined at 0.235-nm resolution by X-ray diffraction. Carboxypeptidase T is a remote homologue of mammalian Zn-carboxypeptidases. In spite of the low degree of ami
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5beb7c2d4f72d1cf202557c4a348e8cd
https://doi.org/10.1111/j.1432-1033.1992.tb17184.x
https://doi.org/10.1111/j.1432-1033.1992.tb17184.x
Autor:
Keith S. Wilson, Michail N. Isupov, Alfred A. Antson, B. V. Strokopytov, E.H. Harutyunyan, Garib N. Murshudov, Howard Terry, Zbigniew Dauter, Tatyana V. Demidkina, Dmitry G. Vassylyev
Publikováno v:
FEBS Letters. 302:256-260
The tyrosine phenol lyase (EC 4.1.99.2) from Citrobacter intermedius has been crystallised in the apo form by vapour diffusion. The space group is P21212. The unit cell has dimensions a = 76.0 Å, b = 138.3 Å, c = 93.5 Å and it contains two subunit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52e3cccf616bf77b3da76df3fe5965cb
https://doi.org/10.1016/0014-5793(92)80454-o
https://doi.org/10.1016/0014-5793(92)80454-o
Autor:
B. V. Strokopytov, Lucy Malinina
Publikováno v:
Journal of biomolecular structuredynamics. 11(5)
A simplified multidimensional search was applied to determine the structure of deoxyhexamer CGCGCG in the crystal form belonging to the space group C222(1) (a = 45.6 A, b = 37.3 A, c = 70.3 A). This crystal form contains two Z-DNA duplexes per asymme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8357b1a7f3470d7bc0707f5676fb0b2
https://pubmed.ncbi.nlm.nih.gov/7946060
https://pubmed.ncbi.nlm.nih.gov/7946060
Publikováno v:
Bioorganicheskaia khimiia. 19(1)
The human progastricsin crystal structure has been solved by the molecular replacement method. The intensities of reflections from native progastricsin crystals were measured at the 4.0 A resolution by the omega-scan method with a Nicolet P3 diffract
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1b00afa362de52dbac4de345d8be58d3
https://pubmed.ncbi.nlm.nih.gov/8484812
https://pubmed.ncbi.nlm.nih.gov/8484812
Autor:
B. V. Strokopytov, Vladimir Popov, Maria G. Yukhnevich, Victor S. Lamzin, E.H. Harutyunyan, Alexander E. Aleshin, Keith S. Wilson
Publikováno v:
European journal of biochemistry. 206(2)
The ternary complex of NAD-dependent formate dehydrogenase (FDH) from the methylotrophic bacterium Pseudomonas sp. 101 (enzyme-NAD-azide) has been crystallised in the space group P2(1)2(1)2(1) with cell dimensions a = 11.60 nm, b = 11.33 nm, c = 6.34
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea154763b6fd0b404481f0aad37c195d
https://pubmed.ncbi.nlm.nih.gov/1597184
https://pubmed.ncbi.nlm.nih.gov/1597184
Publikováno v:
Molekuliarnaia biologiia. 25(4)
An X-ray crystallographic structure determination has been carried out on bovine lens leucine aminopeptidase at 4.0 A resolution by using a combination of isomorphous replacement and solvent flattening. The two heavy atom derivatives used were obtain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::17ee8cd5a54a4af2f7a673c83b7db8d1
https://pubmed.ncbi.nlm.nih.gov/1795703
https://pubmed.ncbi.nlm.nih.gov/1795703
[Structural basis for differences in substrate specificity of aspartate aminotransferase isoenzymes]
Publikováno v:
Molekuliarnaia biologiia. 24(1)
X-Ray structural data concerning the substrate binding site of cytosolic chicken aspartate aminotransferase (AspAT) are reported. The structure of the complex of AspAT with the substrate-like inhibitor maleate has been refined at 2.2 A resolution. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8712d64294b695c70e6cd4277faa04e6
https://pubmed.ncbi.nlm.nih.gov/2348826
https://pubmed.ncbi.nlm.nih.gov/2348826
Autor:
T.Ya. Morozova, G.S. Kachalova, E.T. Myachin, B. V. Strokopytov, A.A. Vagin, Yu. V. Nekrasov, Victor N. Morozov
Publikováno v:
FEBS Letters. (1):91-94
A high resolution structure of hen egg-white lysozyme containing 36 ± I mol H2O per mol of protein has been obtained using triclinic (P1) crystals cross-linked with glutaraldehyde. Analysis of dehydration-induced structural changes has revealed disp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23a27090e79dfe65976c01057ef17049