Crystallization and preliminary X-ray analysis of the 12S central subunit of transcarboxylase from Propionibacterium shermanii.
Crystallization and preliminary X-ray analysis of the 12S central subunit of transcarboxylase from Propionibacterium shermanii.
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谢尔曼丙酸杆菌转羧酶 12S 中心亚基的结晶和初步 X 射线分析。
DOI：
10.1107/s0907444900015237
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发表时间：
2001
期刊：
影响因子：
--
通讯作者：
Yee,VC
中科院分区：
文献类型：
--
作者：
Wang,YF;Hyatt,DC;Rivera,RE;Carey,PR;Yee,VC
The hexameric 12S central subunit of transcarboxylase has been crystallized in both free and substrate-bound forms. The apo crystals belong to the cubic space group P4232, with unit-cell parameters a = b = c = 188.5 Å, and diffract to 3.5 Å resolution. Crystals of two substrate-bound complexes, 12S with methylmalonyl CoA and 12S with malonyl CoA, are isomorphous and belong to space group C2, with unit-cell parameters a = 115.5, b = 201.4, c = 146.9 Å, β = 102.7°. These crystals diffract to 1.9 Å resolution with synchrotron radiation. Two useful heavy-atom phasing derivatives of methylmalonyl CoA-bound crystals have been obtained by co-crystallization or crystal soaking.
