Kuriyan J, Wong L, Russel M, Model P
Rockefeller University, New York 10021.
J Biol Chem. 1989 Aug 5;264(22):12752-3.
Single crystals of thioredoxin reductase, suitable for x-ray diffraction studies, have been obtained at room temperature by vapor diffusion of 10-20 mg/ml protein solution against 35% polyethylene glycol containing 200 mM ammonium sulfate. Good quality crystals appear spontaneously only from a protein solution that had been stored for more than a year at 4 degrees C, although large single crystals are reproducibly obtained from fresh protein solutions by micro-seeding. The space group is P6(3)22 (a = b = 123.8 A, c = 81.6 A), with one monomer of the enzyme (34.5 kDa) in the crystallographic asymmetric unit. The crystals are well ordered and diffract to beyond 2 A resolution.
已通过将10-20毫克/毫升的蛋白质溶液与含有200毫摩尔硫酸铵的35%聚乙二醇进行气相扩散，在室温下获得了适合X射线衍射研究的硫氧还蛋白还原酶单晶。尽管通过微量接种可从新鲜蛋白质溶液中重复获得大的单晶，但高质量的晶体仅自发地从在4摄氏度下储存了一年以上的蛋白质溶液中出现。空间群为P6(3)22（a = b = 123.8埃，c = 81.6埃），晶体学不对称单元中含有一个酶单体（34.5 kDa）。这些晶体排列良好，衍射分辨率超过2埃。
