从酵母中结晶真核生物E3（硫辛酰胺脱氢酶），以获得分辨率超过2.5埃的X射线衍射图谱，并进行初步结构分析。
Crystallization of eukaryotic E3, lipoamide dehydrogenase, from yeast, for exhibiting X-ray diffraction beyond 2.5 A resolution, and preliminary structure analysis.
作者信息
Toyoda T, Sekiguchi T, Takenaka A
机构信息
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama.
出版信息
J Biochem. 1997 Jan;121(1):1-4. doi: 10.1093/oxfordjournals.jbchem.a021550.
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.
硫辛酰胺脱氢酶是α-酮酸脱氢酶复合体的常见组分，已从酵母（酿酒酵母）中高度纯化，以更高分辨率揭示其结构。通过脱盐方法获得的新晶体显示出超过2.5埃分辨率的衍射。晶胞尺寸为a = 97.1、b = 158.7和c = 67.9埃，空间群为P2(1)2(1)2(1)。不对称单元中有一个二聚体酶。晶体结构通过分子置换技术解析并进行了初步精修。
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