在一种新合成的纤维素酶抑制剂存在的情况下，嗜纤维梭菌CeLF纤维素酶催化结构域的结晶。
Crystallization of the catalytic domain of Clostridium cellulolyticum CeLF cellulase in the presence of a newly synthesized cellulase inhibitor.
作者信息
Reverbel-Leroy C, Parsiegla G, Moreau V, Juy M, Tardif C, Driguez H, Bélaich J P, Haser R
机构信息
Université de Provence, Place Victor-Hugo, 13331 Marseille CEDEX 3, France.
出版信息
Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):114-8. doi: 10.1107/s090744499700797x.
The catalytic domain of the CeIF processive endocellulase, a family 48 glycosyl hydrolase from Clostridium cellulolyticum has been crystallized in the presence of a newly synthesized inhibitor (methyl 4-S-beta-cellobiosyl-4-thio-beta-cellobioside), by vapour diffusion, using PEG as a precipitant. The protein crystallizes in the orthorhombic P212121 space group and diffracts to a resolution of 2.0 A. The unit-cell parameters are a = 61.4, b = 84.5, c = 121.9 A.
来自解纤维素梭菌的48家族糖基水解酶CeIF持续性内切纤维素酶的催化结构域，在一种新合成的抑制剂（4-S-β-纤维二糖基-4-硫代-β-纤维二糖苷甲酯）存在的情况下，通过气相扩散法，以聚乙二醇作为沉淀剂进行了结晶。该蛋白质结晶于正交晶系P212121空间群，衍射分辨率为2.0 Å。晶胞参数为a = 61.4，b = 84.5，c = 121.9 Å。
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