Purification, crystallization and preliminary crystallographic analysis of the non-Pfam protein AF1514 from Archeoglobus fulgidus DSM 4304.

Purification, crystallization and preliminary crystallographic analysis of the non-Pfam protein AF1514 from Archeoglobus fulgidus DSM 4304.
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来自 Archeoglobus fulgidus DSM 4304 的非 Pfam 蛋白 AF1514 的纯化、结晶和初步晶体学分析。

DOI:
10.1107/s1744309107068649
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发表时间:
2008
期刊:
Acta crystallographica. Section F, Structural biology and crystallization communications
影响因子:
--
通讯作者:
Liu,ZhiJie
Liu,ZhiJie
中科院分区:
--
文献类型:
--
作者:
Bahti,Pazilat;Chen,Shunmei;Li,Yang;Shaw,Neil;Zhang,Xuejun;Zhang,Min;Cheng,Chongyun;Song,Gaojie;Yin,Jie;Zhang,Hua;Che,Dongsheng;Abbas,Abdulla;Xu,Hao;Wang,BiCheng;Liu,ZhiJie

文献摘要

相似文献

一个10.5 kDa的非Pfam假设的蛋白质,AF1514,从超嗜热古菌Archeoglobus fulgidus已在大肠杆菌中过表达,纯化和结晶使用悬滴气相扩散法。 晶体衍射X射线到2.09 μ m的分辨率和数据集收集在100 K使用铜Kα辐射从一个阳极X射线源。   晶体属空间群P41212或P43212,晶胞参数a = B = 49.27,c = 106.61 Ω. 计算的马修斯系数为3.16 3 Da−1,表明在不对称单元中存在一个分子。  
A 10.5 kDa non-Pfam hypothetical protein, AF1514, from the hyperthermophilic archaeon Archeoglobus fulgidus has been overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted X-rays to 2.09 Å resolution and a data set was collected at 100 K using Cu Kα radiation from a rotating-anode X-ray source. The crystals belong to space group P41212 or P43212, with unit-cell parameters a = b = 49.27, c = 106.61 Å. The calculated Matthews coefficient was 3.16 Å3 Da−1, suggesting the presence of one molecule in the asymmetric unit.