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Crystallization and preliminary X‐ray crystallographic analysis of arylesterase from vibrio mimicus
Author(s) -
Musayev Faik N.,
Lee YaLin,
Shaw JeFu,
Liaw YenChywan
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560040928
Subject(s) - monoclinic crystal system , crystallization , crystallography , arylesterase , ammonium sulfate , resolution (logic) , molecule , chemistry , solvent , x ray crystallography , vibrio , diffraction , crystal structure , biology , bacteria , biochemistry , physics , chromatography , organic chemistry , genetics , optics , gene , pon1 , artificial intelligence , computer science , genotype
Single crystals of arylesterase (EC 3.1.1.2) from Vibrio mimicus have been obtained from ammonium sulfate as a precipitant at room temperature for 2 months. The present crystals diffract up to 2.2 Å resolution and belong to monoclinic space group P2 1 . The cell dimensions are a = 55.65(1) Å, b = 53.46(1) Å, c = 65.79(1) Å, and β = 106.54(1)°. There are two molecules of molecular weight 22 kDa in an asymmetric unit with a solvent content of 43%.