Crystallization and preliminary X-ray crystallographic analysis of the 30 kDa membrane-binding domain of protein 4.1 from human erythrocytes

Bong-Gyoon Han; Wataru Nunomura; Huiying WuNarla MohandasBing K. Jap

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Crystallization and preliminary X-ray crystallographic analysis of the 30 kDa membrane-binding domain of protein 4.1 from human erythrocytes

机译：结晶和初步的x射线晶体的分析30 kDa从人类membrane-binding域蛋白质4.1红细胞

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摘要

The 30 kDa membrane-binding domain of protein 4.1 from human erythrocytes has been expressed in Escherichia coli and crystallized in a form suitable for X-ray crystallographic study. Crystals were grown using a salting-in technique. Crystals have a tetragonal plate shape and belong to the C2 space group, with unit-cell parameters a = 163.9, b = 106.5, c = 93.5 A, β = 95.5 °. The crystals diffract to 2.8 A resolution.

机译：4.1 30 kDa membrane-binding域的蛋白质从人类红细胞中表达大肠杆菌和结晶形式适合x射线晶体研究。晶体使用salting-in种植技术。晶体有正方板形状和归属感C2空间群,晶胞参数b = 106.5 = 163.9, c = 93.5,β= 95.5°。晶体衍射分辨率2.8。

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《Acta crystallographica.Section D. Biological crystallography》 |2000年第2期|187-188|共2页
作者
Bong-Gyoon Han; Wataru Nunomura; Huiying WuNarla MohandasBing K. Jap;
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作者单位

Department of Biochemistry, Tokyo Women's Medical University, Tokyo 162-8666, Japan;

Life Sciences Division, Lawrence Berkeley National Laboratory, University of California, Berkeley, California 94720, USA;

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正文语种英语
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Hematocrit; crystals; Proteinspace groupsDomainX-raysprotein domainCrystallization;

机译：血细胞比容;晶体;ProteinspacegroupsDomainX-raysprotein domainCrystallization;

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Crystallization and preliminary X-ray crystallographic analysis of the 30 kDa membrane-binding domain of protein 4.1 from human erythrocytes

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