Crystallization of eukaryotic E3, lipoamide dehydrogenase, from yeast, for exhibiting X-ray diffraction beyond 2.5 A resolution, and preliminary structure analysis.
Lipoamide dehydrogenase, which is a common component of alpha-keto acid dehydrogenase complexes, has been highly purified from yeast (Saccharomyces cerevisiae) to reveal its structure at higher resolution. New crystals obtained by a desalting method exhibited diffraction beyond 2.5 A resolution. The cell dimensions are a = 97.1, b = 158.7, and c = 67.9 A, and the space group is P2(1)2(1)2(1). There is a dimeric enzyme in the asymmetric unit. The crystal structure was solved by means of the molecular-replacement technique and refined in a preliminary manner.
Toyoda
T
T
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama.
Sekiguchi
T
T
Takenaka
A
A
D003460:Crystallization; D018360:Crystallography, X-Ray; D008058:Dihydrolipoamide Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000201:enzymology*; D013053:Spectrophotometry
D008058:Dihydrolipoamide Dehydrogenase