Crystallization and preliminary X-ray studies of Pseudomonas putida histidine ammonium-lyase.
Crystallization and preliminary X-ray studies of Pseudomonas putida histidine ammonium-lyase.
复制标题
恶臭假单胞菌组氨酸铵裂解酶的结晶和初步 X 射线研究。
DOI：
10.1107/s0907444997017848
复制
发表时间：
1998
期刊：
影响因子：
--
通讯作者：
Farber,GK
中科院分区：
文献类型：
--
作者：
Teo,B;Kidd,RD;Mack,J;Tiwari,A;Hernandez,D;Phillips,AT;Farber,GK
在大肠杆菌中表达了恶臭假单胞菌的组氨酸解氨酶，纯化至均一，并使用聚乙二醇3350作为沉淀剂通过气相扩散法结晶。该晶体具有空间群P212121的对称性，晶胞参数a = 89.7，B = 138.2，c = 164.8。 不对称单元包含一个四聚体，晶体的Vm值为2.41 <$3 Da−1。
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 Å resolution, exhibit the symmetry of space group P212121, with unit-cell parameters a = 89.7, b = 138.2 and c = 164.8 Å. The asymmetric unit contains a tetramer, and the crystals have a Vm value of 2.41 Å3 Da−1.