Zobrazeno 1 - 10 of 44 pro vyhledávání: '"P. F. Lindley"'
1
Three-dimensional structure of laccase from Coriolus zonatus at 2.6 Å resolution
Autor: Azat Gabdulkhakov, Al'bert M. Mikhailov, A. V. Lyashenko, Elena V. Stepanova, I. Bento, Vladimir I. Tishkov, Yu. N. Zhukova, N. E. Zhukhlistova, Ch. Betzel, P. F. Lindley, E. Yu. Morgunova, O. V. Koroleva, Wolfang Voelter, Galina S. Kachalova, Viatcheslav Zaitsev
Publikováno v: Crystallography Reports. 51:817-823
Laccase (oxygen oxidoreductase, EC 1.14.18.1) belongs to the copper-containing oxidases. This enzyme catalyzes reduction of molecular oxygen by different organic and inorganic compounds to water without the formation of hydrogen peroxide. The three-d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cb21c0aa989857b2242fbaecc98d35d8
https://doi.org/10.1134/s1063774506050117
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2
High-resolution neutron study of vitamin B12 coenzyme at 15 K: structure analysis and comparison with the structure at 279 K
Autor: M. S. Lehmann, J. L. Finney, H. F. J. Savage, J. P. Bouquiere, P. F. Lindley
Publikováno v: Acta Crystallographica Section B Structural Science. 49:79-89
C72H100N18O17PCo.nH2O, where n = 17-18, M(r) = 1597 dalton (assuming that 19 coenzyme H atoms have been exchanged for D atoms), P2(1)2(1)2(1), a = 27.550 (7), b = 21.568 (5), c = 15.343 (3) angstrom, V = 9117 (4) angstrom3, Z = 4, D(x) = 1.38 (1) Mg
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::69ed82291dfd34818037841824437a84
https://doi.org/10.1107/s0108768192007511
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3
Structure of a low-temperature polymorph of chenodeoxycholic acid, C24H40O4, determined with synchrotron radiation
Autor: P. J. Rizkallah, M. M. Harding, A. Bauer, A. Aigner, P. F. Lindley
Publikováno v: Acta Crystallographica Section B Structural Science. 46:262-266
Le polymorphisme a basse temperature de C 24 H 40 O 4 cristallise dans P6 5 , avec a=22,250, c=10,255 A, Z=6, affinement jusqu'a R=0,11. Tous les atomes d'oxygene participent a des liaisons hydrogene intermoleculaires
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d3ea8ebca960c9e9ec721d28c168a2bd
https://doi.org/10.1107/s010876818901195x
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5
Mounting and setting of specimens for X-ray crystallographic studies
Autor: P. F. Lindley
Publikováno v: International Tables for Crystallography ISBN: 9781402019005
International Tables for Crystallography
This chapter describes the mounting of both polycrystalline specimens (powders) and single crystals for recording X-ray diffraction patterns. It also deals with the handling of specimens under extreme conditions of both high and low temperature and t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2b1af6cbbc899205f01a5972607e39bf
https://doi.org/10.1107/97809553602060000588
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6
The 'prismane' protein resolved: X-ray structure at 1.7A and multiple spectroscopy of two novel 4Fe clusters
Autor: Alexander F. Arendsen, Jonathan Hadden, Graeme Card, Alan S. McAlpine, Susan Bailey, Vjacheslav Zaitsev, Elizabeth H. M. Duke, P. F. Lindley, Monika Kröckel, Alfred X. Trautwein, Martinus C. Feiters, John M. Charnock, C. David Garner, Sophie J. Marritt, Andrew J. Thomson, Ingeborg M. Kooter, Michael K. Johnson, Willy A. M. van den Berg, Walter M. A. M. van Dongen, W. R. Hagen
Publikováno v: Journal of Biological Inorganic Chemistry 3 (1998)
Journal of Biological Inorganic Chemistry, 3, 81-95
The three-dimensional structure of the native "putative prismane" protein from Desulfovibrio vulgaris (Hildenborough) has been solved by X-ray crystallography to a resolution of 1.72 A. The molecule does not contain a [6Fe-6S] prismane cluster, but r
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c63632b4957ee26626b3180c1126679
https://research.wur.nl/en/publications/the-prismane-protein-resolved-x-ray-structure-at-17a-and-multiple
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7
Structure of bovine eye lens gammaD (gammaIIIb)-crystallin at 1.95 A
Autor: Y N, Chirgadze, H P, Driessen, G, Wright, C, Slingsby, R E, Hay, P F, Lindley
Publikováno v: Acta crystallographica. Section D, Biological crystallography. 52(Pt 4)
The crystal structure of bovine lens gammaIIIb-crystallin at 2.5 A resolution previously reported was interpreted using a consensus sequence derived from related vertebrate sequences on the assumption that gammaIIIb-crystallin derived from the gammaC
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ee7cbfb84b2af9d2deb1bdc0ac06370a
https://pubmed.ncbi.nlm.nih.gov/15299634
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8
Asp ligand provides the trigger for closure of transferrin molecules. Direct evidence from X-ray scattering studies of site-specific mutants of the N-terminal half-molecule of human transferrin
Autor: J G, Grossmann, A B, Mason, R C, Woodworth, M, Neu, P F, Lindley, S S, Hasnain
Publikováno v: Journal of molecular biology. 231(3)
Recent X-ray crystallographic and solution X-ray scattering studies have shown that transferrins (serum transferrin, lactoferrin and ovotransferrin) undergo a major conformational change when iron is incorporated into the molecule. Apo-proteins show
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d50bd98a55be98b80ae39520621094ab
https://pubmed.ncbi.nlm.nih.gov/8515439
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9
Structure of the bovine eye lens protein gammaB(gammaII)-crystallin at 1.47 A
Autor: S, Najmudin, V, Nalini, H P, Driessen, C, Slingsby, T L, Blundell, D S, Moss, P F, Lindley
Publikováno v: Acta crystallographica. Section D, Biological crystallography. 49(Pt 2)
The molecular structure of calf gammaB-crystallin (previously called gammaII), a lens-specific protein, has been refined to a crystallographic R factor of 18.1% for all reflection data, between 8.0 and 1.47 A, 25 959 hkl measured at 293 (1) K. 230 wa
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::befc7b88dba5bf1b01c146fea47b976e
https://pubmed.ncbi.nlm.nih.gov/15299528
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10
High resolution structure of an oligomeric eye lens beta-crystallin. Loops, arches, linkers and interfaces in beta B2 dimer compared to a monomeric gamma-crystallin
Autor: R, Lapatto, V, Nalini, B, Bax, H, Driessen, P F, Lindley, T L, Blundell, C, Slingsby
Publikováno v: Journal of molecular biology. 222(4)
beta-Crystallins are polydisperse, oligomeric structural proteins that have a major role in forming the high refractive index of the eye lens. Using single crystal X-ray crystallography with molecular replacement, the structure of beta B2 dimer has b
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::35a1fb0308b7a449a2ff2ab701741b25
https://pubmed.ncbi.nlm.nih.gov/1762146
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