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Crystallization and preliminary X‐ray diffraction study of 1,3,8‐trihydroxynaphthalene reductase from Magnaporthe grisea
Author(s) -
Andersson Arnold,
Jordan Doug,
Schneider Gunter,
Valent Barbara,
Lindqvist Ylva
Publication year - 1996
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199604)24:4<525::aid-prot14>3.0.co;2-n
Subject(s) - crystallography , crystallization , resolution (logic) , crystal (programming language) , diffraction , trigonal crystal system , reductase , magnaporthe grisea , chemistry , crystal structure , stereochemistry , physics , enzyme , optics , biochemistry , gene , computer science , oryza sativa , organic chemistry , artificial intelligence , programming language
Abstract 1,3,8‐Trihydroxynaphthalene reductase was crystallized in the presence of NADPH and the inhibitor tricyclazole. The crystals are trigonal, space group P3 1 21 or its enantiomorph P3 2 21. Two crystal forms with slightly different cell dimensions were obtained. Form A has unit cell dimensions a = b = 142.6 Å, c = 70.1 Å and form B cell dimensions a = b = 142.6 Å, c = 72.9 Å. The diffraction pattern of the latter crystal form extends to 2.5 Å resolution.