谷氨酸棒杆菌中内消旋二氨基庚二酸脱氢酶的表达、纯化及结晶
Expression, purification, and crystallization of meso-diaminopimelate dehydrogenase from Corynebacterium glutamicum.
作者信息
Reddy S G, Scapin G, Blanchard J S
机构信息
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
出版信息
Proteins. 1996 Aug;25(4):514-6. doi: 10.1002/prot.12.
The gene encoding the meso-diaminopimelate dehydrogenase (DAPDH) from Corynebacterium glutamicum was over-expressed and purified to homogeneity. Crystals of the binary DAPDH-NADP+ complex were obtained from solutions of polyethylene glycol 8000, 100 mM sodium cacodylate, pH 6.5, and 150-300 mM Mg(OAc)2. The crystals diffract to 2.2 A, belong to the orthorhombic space group P2(1), and contain two molecules per asymmetric unit.
来自谷氨酸棒杆菌的中-二氨基庚二酸脱氢酶（DAPDH）编码基因被过表达并纯化至同质。二元DAPDH-NADP⁺复合物的晶体是从含有聚乙二醇8000、100 mM二甲胂酸钠（pH 6.5）和150 - 300 mM乙酸镁的溶液中获得的。这些晶体的衍射分辨率为2.2 Å，属于正交晶系空间群P2(1)，每个不对称单元包含两个分子。
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