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嗜热古菌嗜热栖热放线菌来源的L-丝氨酸3-脱氢酶与NADP⁺复合物的结晶及初步X射线分析

Crystallization and preliminary X-ray analysis of L-serine 3-dehydrogenase complexed with NADP+ from the hyperthermophilic archaeon Pyrobaculum calidifontis.

作者信息

Yoneda Kazunari, Sakuraba Haruhiko, Araki Tomohiro, Shibata Takeshi, Nikki Takahiro, Ohshima Toshihisa

机构信息

Department of Bioscience, School of Agriculture, Tokai University, Aso, Kumamoto 869-1404, Japan.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Feb 1;69(Pt 2):134-6. doi: 10.1107/S1744309112051391. Epub 2013 Jan 31.

DOI:10.1107/S1744309112051391
PMID:23385753
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3564614/
Abstract

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 Å, β = 106.88°. Diffraction data were collected to 1.57 Å resolution on beamline NE3A at the Photon Factory. The overall R(merge) was 4.2% and the data completeness was 90.1%.

摘要

利用坐滴气相扩散法,以硫酸铵作为沉淀剂,对嗜热古菌嗜热栖热放线菌(Pyrobaculum calidifontis)中一种依赖NAD(P)(+)的L-丝氨酸3-脱氢酶进行了结晶。晶体属于单斜晶系空间群C2,晶胞参数为a = 120.81,b = 57.40,c = 56.37 Å,β = 106.88°。在光子工厂的NE3A光束线上收集了分辨率为1.57 Å的衍射数据。整体合并R值为4.2%,数据完整性为90.1%。

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引用本文的文献

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