Premium
Crystallization and preliminary X‐ray crystallographic studies of L ‐2‐haloacid dehalogenase from Pseudomonas sp. YL
Author(s) -
Hisano Tamao,
Hata Yasuo,
Fujii Tomomi,
Liu JiQuan,
Kurihara Tatsuo,
Esaki Nobuyoshi,
Soda Kenji
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<520::aid-prot12>3.0.co;2-n
Subject(s) - crystallization , dehalogenase , crystallography , chemistry , x ray , biochemistry , enzyme , physics , organic chemistry , quantum mechanics
The dimeric L ‐2‐haloacid dehalogenase from Pseudomonas sp. YL, (subunit mass, 26179 Da), has been crystallized by vapor diffusion, supplemented by repetitive seeding, against a 50 mM potassium dihydrogenphosphate solution (pH 4.5) containing 15% (w/v) polyethylene glycol 8,000 and 1% (v/v) n ‐propanol. The crystals belong to the monoclinic space group C 2 with unit cell dimensions of a = 92.21 Å, b = 62.78 Angst; c = 50.84 Å, and β = 122.4°, and contain two dehalogenase dimers in the unit cell. They are of good quality and diffract up to 1.5 Å resolution.