GreA（一种来自大肠杆菌的转录切割因子）的结晶。
Crystallization of GreA, a transcript cleavage factor from Escherichia coli.
作者信息
Darst S A, Stebbins C E, Borukhov S, Orlova M, Feng G, Landick R, Goldfarb A
机构信息
Rockefeller University, New York, NY 10021.
出版信息
J Mol Biol. 1994 Sep 30;242(4):582-5. doi: 10.1006/jmbi.1994.1603.
GreA is a 17.6 kDa protein from Escherichia coli that induces cleavage of the nascent transcript in the elongating complex of RNA polymerase, followed by release of the 3'-terminal fragment. Crystals of GreA have been obtained from polyethylene glycol 4000, 2-propanol and sodium citrate, pH 5.6 and have been propagated by a novel seeding procedure. The crystals diffract beyond 2 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with cell dimensions a = 101.7 A, b = 42.22 A, c = 40.05 A and with one molecule in the asymmetric unit.
GreA是一种来自大肠杆菌的17.6 kDa蛋白质，它能诱导RNA聚合酶延伸复合物中新生转录本的切割，随后释放3'末端片段。GreA晶体已从聚乙二醇4000、异丙醇和柠檬酸钠（pH 5.6）中获得，并通过一种新颖的接种程序进行传代培养。这些晶体的衍射分辨率超过2 Å，属于正交空间群P2(1)2(1)2(1)，晶胞参数a = 101.7 Å，b = 42.22 Å，c = 40.05 Å，不对称单位中有一个分子。
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