Crystallization of and Preliminary Crystallographic Data for Allosteric L-Lactate Dehydrogenase from Bifidobacterium longum1
- 1 October 1989
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 106 (4) , 558-559
- https://doi.org/10.1093/oxfordjournals.jbchem.a122894
Abstract
L-Lactate dehydrogenase from BiUdobacterium longum aM101–2 was overexpressed in Escherichia coli and then purified. The enzyme was crystallized from a polyethylene glycol 6000 solution by the hanging drop vapor diffusion method. Crystals grown in the presence of NADH (type II), both NADH and oxamate (type III), and NADH, oxamate, and FBP (type IV) were analyzed. All three crystal forms belong to the orthorhombic system, space group P21212. The cell dimensions of the type II crystals were a=106.2 A, 6 = 131.6 A, and c = 63.8 A. Those of the type III and type IV crystals were a = 106.4 A, 6 = 131.4 A, and c = 63.8 A. The type HI crystals diffract X-rays to beyond 2.5 A spacing. The type II and type HI crystals were stable as to X-ray irradiation.This publication has 5 references indexed in Scilit:
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