Crystallization and preliminary X‐ray diffraction study of 1,3,8‐trihydroxynaphthalene reductase from  Magnaporthe grisea | Zendy

Andersson Arnold | Zendy; Jordan Doug | Zendy; Schneider Gunter | Zendy; Valent Barbara | Zendy; Lindqvist Ylva | Zendy

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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

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.

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