Kinoshita T, Tada T, Saito Y, Ishii Y, Sato A, Murata M
Basic Research Laboratories, Fujisawa Pharmaceutical Co. Ltd, 1-6 Kashima 2-Chome, Yodogawa-ku, Osaka 532-8514, Japan.
Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):458-9. doi: 10.1107/s0907444900000718.
Cephalosporin C acylase from Pseudomonas sp. strain N176, a heterodimer of 25 and 58 kDa, has been crystallized using polyethylene glycol 6000 as precipitant. The crystals are orthorhombic and have unit-cell parameters a = 141.41, b = 192.10, c = 80.75 A. They belong to space group P2(1)2(1)2(1) and diffract to at least 2.7 A resolution. Calculations indicate that there are two heterodimers in the asymmetric unit. The structure is being solved by molecular replacement using penicillin G acylase from Escherichia coli as a search model and by multiple isomorphous replacement.
来自假单胞菌属菌株N176的头孢菌素C酰基转移酶是一种由25 kDa和58 kDa组成的异源二聚体，已使用聚乙二醇6000作为沉淀剂进行了结晶。晶体为正交晶系，晶胞参数a = 141.41，b = 192.10，c = 80.75 Å。它们属于空间群P2(1)2(1)2(1)，衍射分辨率至少为2.7 Å。计算表明，不对称单元中有两个异源二聚体。该结构正在通过以大肠杆菌青霉素G酰基转移酶为搜索模型的分子置换法和多重同晶置换法来解析。
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