Crystallization of allosteric L-lactate dehydrogenase from Thermus caldophilus and preliminary crystallographic data.
L-Lactate dehydrogenase of Thermus caldophilus GK24 was purified from Escherichia coli containing an overexpression plasmid. The enzyme was crystallized from polyethylene glycol 6000 solutions without ligands by the hanging drop vapor diffusion method. Two forms of crystals were obtained. The crystals grown at pH 6.0 were characterized by means of an X-ray diffraction experiment, while those grown at pH 6.5 and 7.0 did not give detectable diffraction spots. The crystals grown at pH 6.0 belonged to monoclinic space group P2(1), the cell dimensions being a = 54.8 A, b = 138.2A, c = 86.1 A, and beta = 93.3 degrees. These crystals diffract to beyond 2.5 A spacing and are stable on X-ray irradiation.
Koide
S
S
Department of Agricultural Chemistry, University of Tokyo.
Iwata
S
S
Matsuzawa
H
H
Ohta
T
T
D000494:Allosteric Regulation; D003460:Crystallization; D007770:L-Lactate Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification*; D015394:Molecular Structure; D013824:Thermus / Q000201:enzymology*; D014961:X-Ray Diffraction
D007770:L-Lactate Dehydrogenase