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Crystallization and preliminary X‐ray diffraction studies of a bacterial flavohemoglobin protein
Author(s) -
Ermler Ulrich,
Siddiqui Roman A.,
Cramm Rainer,
Friedrich Bärbel,
Schröder Dirk
Publication year - 1995
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/prot.340210408
Subject(s) - monoclinic crystal system , crystallization , resolution (logic) , crystallography , x ray crystallography , heme , chemistry , molecule , peg ratio , protein crystallization , materials science , diffraction , crystal structure , biochemistry , organic chemistry , optics , enzyme , physics , artificial intelligence , computer science , finance , economics
A flavohemoglobin protein (FHP) was isolated from Alcaligenes eutrophus and has been crystallized by vapor diffusion methods using PEG 3350 as precipitant. The crystals of the FAD‐ and heme‐containing protein belong to the monoclinic space group P 2 1 with unit cell parameters of 52.2 Å, 85.8 Å, 103.9 Å, and 81.8° corresponding to two molecules per asymmetric unit. The crystals diffract at least to a resolution of 2.0 Å and are suitable for an X‐ray structure analysis. © 1995 Wiley‐Liss, Inc.