首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Crystallization and preliminary X-ray analysis of L-serine 3-dehydrogenase complexed with NADP(+) from the hyperthermophilic archaeon Pyrobaculum calidifontis
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Crystallization and preliminary X-ray analysis of L-serine 3-dehydrogenase complexed with NADP(+) from the hyperthermophilic archaeon Pyrobaculum calidifontis

机译:与超高温古细菌Pyrobaculum calidifontis的NADP(+)结合的L-丝氨酸3-脱氢酶的结晶和初步X射线分析

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摘要

An NAD(P)(+)-dependent l-serine 3-dehydrogenase from the hyperthermophilic archaeon Pyrobaculum calidifontis was crystallized using the sitting-drop vapour-diffusion method with ammonium sulfate as the precipitant. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 120.81, b = 57.40, c = 56.37 angstrom, beta = 106.88 degrees. Diffraction data were collected to 1.57 angstrom resolution on beamline NE3A at the Photon Factory. The overall R-merge was 4.2% and the data completeness was 90.1%.
机译:NAD(P)(+)依赖的L-丝氨酸3-脱氢酶从超嗜热古细菌Pyrobaculum calidifontis中析出,采用坐滴蒸汽扩散法,以硫酸铵为沉淀剂。晶体属于单斜晶空间群C2,单位晶胞参数a = 120.81,b = 57.40,c = 56.37埃,β= 106.88度。在光子工厂,在光束线NE3A上收集了衍射数据,分辨率为1.57埃。总体R合并为4.2%,数据完整性为90.1%。

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