恶臭假单胞菌组氨酸氨裂解酶的结晶及初步X射线研究
Crystallization and preliminary X-ray studies of Pseudomonas putida histidine ammonium-lyase.
作者信息
Teo B, Kidd R D, Mack J, Tiwari A, Hernandez D, Phillips A T, Farber G K
机构信息
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, 108 Althouse Laboratory, University Park, PA 16802, USA.
出版信息
Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):681-3. doi: 10.1107/s0907444997017848.
Histidine ammonium-lyase from P. putida was expressed in Escherichia coli, purified to homogeneity, and crystallized by the vapour-diffusion method using polyethylene glycol 3350 as the precipitant. The crystals, which diffract to at least 2.5 A resolution, exhibit the symmetry of space group P212121, with unit-cell parameters a = 89.7, b = 138.2 and c = 164.8 A. The asymmetric unit contains a tetramer, and the crystals have a Vm value of 2.41 A3 Da-1.
恶臭假单胞菌的组氨酸氨裂解酶在大肠杆菌中表达，纯化至同质，并采用气相扩散法，以聚乙二醇3350作为沉淀剂进行结晶。这些晶体的衍射分辨率至少为2.5 Å，呈现出空间群P212121的对称性，晶胞参数a = 89.7 Å、b = 138.2 Å和c = 164.8 Å。不对称单元包含一个四聚体，晶体的Vm值为2.41 Å3 Da-1。
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