Obmolova G, Badet-Denisot M A, Badet B, Teplyakov A
European Molecular Biology Laboratory, c/o DESY, Hamburg, Germany.
J Mol Biol. 1994 Oct 7;242(5):703-5. doi: 10.1006/jmbi.1994.1619.
The glutamine amidohydrolase and fructose 6-phosphate binding domains of glucosamine-6-phosphate synthase from Escherichia coli have been overexpressed, purified and crystallized for X-ray diffraction analysis. The crystals of the glutamine amidohydrolase domain belong to the orthorhombic space group P2(1)2(1)2(1) with cell dimensions a = 70.4 A, b = 82.5 A, c = 86.1 A, with two molecules in the asymmetric unit, and diffract to 1.9 A resolution. The native Patterson indicated pseudo c-face centering of the unit cell. The fructose 6-phosphate binding domain was crystallized in the hexagonal space group P6(1) or P6(5) with cell dimensions a = b = 63.5 A, c = 334.3 A and with two molecules in the asymmetric unit. Diffraction data to 2.6 A resolution have been collected.
来自大肠杆菌的6-磷酸葡萄糖胺合酶的谷氨酰胺酰胺水解酶和6-磷酸果糖结合结构域已被过量表达、纯化并结晶，用于X射线衍射分析。谷氨酰胺酰胺水解酶结构域的晶体属于正交空间群P2(1)2(1)2(1)，晶胞参数为a = 70.4 Å，b = 82.5 Å，c = 86.1 Å，不对称单元中有两个分子，衍射分辨率为1.9 Å。原生帕特森图表明晶胞具有假c面心。6-磷酸果糖结合结构域在六方空间群P6(1)或P6(5)中结晶，晶胞参数为a = b = 63.5 Å，c = 334.3 Å，不对称单元中有两个分子。已收集到分辨率为2.6 Å的衍射数据。
