酿酒酵母高丝氨酸脱氢酶的结晶及初步X射线衍射研究。
Crystallization and preliminary X-ray diffraction studies of homoserine dehydrogenase from Saccharomyces cerevisiae.
作者信息
DeLaBarre B, Jacques S L, Pratt C E, Ruth D A, Wright G D, Berghuis A M
机构信息
Department of Biochemistry, McMaster University, 1200 Main St West, Hamilton, Ontario L8N 3Z5, Canada.
出版信息
Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):413-5. doi: 10.1107/s0907444997011967.
Recombinant homoserine dehydrogenase from Saccharomyces cerevisiae has been crystallized in three different forms. Crystals of the apo-enzyme belong to the tetragonal space group P4 and have unit-cell-dimensions a = b = 130 and c = 240 A. The resolution limit for these crystals is 3.9 A. Crystals of homoserine dehydrogenase grown in the presence of the co-factor NAD+ have the tetragonal space group P41212 or its enantiomorph P43212. The unit-cell dimensions for these crystals are a = b = 80.4 and c = 250.2 A, and the observed resolution limit is 2.2 A. Protein crystals grown in the presence of the product L-homoserine and the inert NAD+ analogue 3-aminopyridine adenine dinucleotide belong to the monoclinic space group P21 with unit-cell parameters a = 58.8, b = 104.2, c = 120.7 A, beta = 91.9 degrees. This last crystal form has a diffraction limit of 2.7 A resolution.
来自酿酒酵母的重组高丝氨酸脱氢酶已以三种不同形式结晶。脱辅基酶的晶体属于四方晶系空间群P4，晶胞参数a = b = 130 Å，c = 240 Å。这些晶体的分辨率极限为3.9 Å。在辅因子NAD⁺存在下生长的高丝氨酸脱氢酶晶体具有四方晶系空间群P4₁2₁2或其对映体P4₃2₁2。这些晶体的晶胞参数a = b = 80.4 Å，c = 250.2 Å，观察到的分辨率极限为2.2 Å。在产物L-高丝氨酸和惰性NAD⁺类似物3-氨基吡啶腺嘌呤二核苷酸存在下生长的蛋白质晶体属于单斜晶系空间群P2₁，晶胞参数a = 58.8 Å，b = 104.2 Å，c = 120.7 Å，β = 91.9°。最后这种晶体形式的衍射极限为2.7 Å分辨率。
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