Hisano T, Hata Y, Fujii T, Liu J Q, Kurihara T, Esaki N, Soda K
Institute for Chemical Research, Kyoto University, Japan.
Proteins. 1996 Apr;24(4):520-2. doi: 10.1002/(SICI)1097-0134(199604)24:4<520::AID-PROT12>3.0.CO;2-N.
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 C2 with unit cell dimensions of a = 92.21 angstrom, b = 62.78 angstrom, c = 50.84 angstrom, and beta = 122.4 degrees, and contain two dehalogenase dimers in the unit cell. They are of good quality and diffract up to 1.5 angstrom resolution.
来自假单胞菌属YL的二聚体L-2-卤代酸脱卤酶(亚基质量为26179道尔顿),通过气相扩散法,并辅以重复接种,在含有15%(w/v)聚乙二醇8000和1%(v/v)正丙醇的50 mM磷酸二氢钾溶液(pH 4.5)中结晶。晶体属于单斜晶系空间群C2,晶胞参数为a = 92.21埃,b = 62.78埃,c = 50.84埃,β = 122.4°,晶胞中含有两个脱卤酶二聚体。它们质量良好,衍射分辨率可达1.5埃。