Crystallization and preliminary X-ray analysis of pig E3, lipoamide dehydrogenase.
Pig heart lipoamide dehydrogenase was crystallized by the hanging-drop vapor-diffusion method. X-ray diffraction patterns show that the hexagonal crystals have unit-cell dimensions of a = b = 359. 3, c = 140.5 A. The crystal structure has been preliminarily solved by the molecular-replacement method in the space group P6322. Three dimeric molecules have been found in the asymmetric unit, one of them located on the crystallographic twofold axis.
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Midori-ku, Yokohama 226, Japan.
T
T
Toyoda
R
R
Kobayashi
T
T
Sekiguchi
K
K
Koike
M
M
Koike
A
A
Takenaka
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D008058:Dihydrolipoamide Dehydrogenase / Q000737:chemistry*; D009124:Muscle Proteins / Q000737:chemistry; D009206:Myocardium / Q000737:chemistry; D011487:Protein Conformation; D011768:Pyruvate Dehydrogenase Complex / Q000737:chemistry*; D013552:Swine
D009124:Muscle Proteins; D011768:Pyruvate Dehydrogenase Complex; D008058:Dihydrolipoamide Dehydrogenase