Nichols C E, Cocklin S, Dodds A, Ren J, Lamb H, Hawkins A R, Stammers D K
Structural Biology Division, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, England.
Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1722-5. doi: 10.1107/s090744490101410x. Epub 2001 Oct 25.
The NmrA repressor protein of Aspergillus nidulans was overproduced in Escherichia coli and purified to homogeneity. Gel-exclusion chromatography showed that NmrA was monomeric in solution under the buffer conditions used. The protein was crystallized in three forms, belonging to trigonal, monoclinic and hexagonal space groups. Two of these crystal forms (A and B) diffract to high resolution and thus appear suitable for structure determination. Crystal form A belongs to space group P3((1))21, with unit-cell parameters a = b = 76.8, c = 104.9 A. Crystal form B belongs to space group C2, with unit-cell parameters a = 148.8, b = 64.3, c = 110.2 A, beta = 121.8 degrees.
构巢曲霉的NmrA阻遏蛋白在大肠杆菌中过量表达并纯化至同质。凝胶排阻色谱显示，在所使用的缓冲液条件下，NmrA在溶液中呈单体形式。该蛋白以三种形式结晶，分别属于三方、单斜和六方空间群。其中两种晶体形式（A和B）衍射至高分辨率，因此似乎适合进行结构测定。晶体形式A属于空间群P3(1)21，晶胞参数a = b = 76.8，c = 104.9 Å。晶体形式B属于空间群C2，晶胞参数a = 148.8，b = 64.3，c = 110.2 Å，β = 121.8°。
