Roig V, Fierobe H P, Ducros V, Czjzek M, Belaich A, Gaudin C, Belaich J P, Haser R
Laboratoire de Cristallographie et Cristallisation des Macro-molécules Biologiques CNRS URA 1296, Université d'Aix-Marseille II, Faculté de Médecine Nord, France.
J Mol Biol. 1993 Sep 20;233(2):325-7. doi: 10.1006/jmbi.1993.1512.
The catalytic domain of an endoglucanase belonging to family A (CelCCA) from an anaerobic bacterium (Clostridium cellulolyticum) has been crystallized in a form suitable for X-ray diffraction analysis. The crystals have been grown in the presence of polyethylene glycol 4000 using the vapour diffusion technique. The crystals, which diffract to 2.0 A resolution, belong to the orthorhombic space group P2(1)2(1)2(1) and have the following cell constants: a = 52.4 A, b = 76.2 A and c = 113.5 A.
来自厌氧细菌(解纤维素梭菌)的A家族内切葡聚糖酶(CelCCA)的催化结构域已结晶成适合X射线衍射分析的形式。晶体是在聚乙二醇4000存在下使用气相扩散技术生长的。这些晶体的衍射分辨率为2.0埃,属于正交空间群P2(1)2(1)2(1),具有以下晶胞常数:a = 52.4埃,b = 76.2埃,c = 113.5埃。