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.
Toyoda
T
T
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Midori-ku, Yokohama 226, Japan.
Kobayashi
R
R
Sekiguchi
T
T
Koike
K
K
Koike
M
M
Takenaka
A
A
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