Human apolipoprotein A-I: structure determination and analysis of unusual diffraction characteristics.

Borhani DW; Brouillette CG; Engler JA

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Human apolipoprotein A-I: structure determination and analysis of unusual diffraction characteristics.

机译：人类载脂蛋白-ⅰ:结构的决心和分析不寻常的衍射特征。

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The crystallization and structure determination of recombinant human apolipoprotein A-I (apo A-I), the major protein component of high-density lipoprotein, is described. The fragment crystallized, residues 44-243 of native apo A-I [apo Delta(1-43)A-I], is very similar to intact native apo A-I in its ability to bind lipid, to be incorporated into high-density lipoproteins and to activate lecithin-cholesterol acyl transferase. Apo Delta(1-43)A-I crystallizes from 1.0-1.4 M sodium citrate pH 6.5-7.5 in space group P2(1)2(1)2(1), with unit-cell parameters a = 97.47, b = 113.87, c = 196.19 A (crystal form I). The crystals exhibit unusual diffraction intensity spikes and axial extinctions that are discussed in the context of the 4 A crystal structure. When flash-cooled to 100 K, the crystals diffract synchrotron radiation to 3 A resolution. Radiation sensitivity and crystal-to-crystal variation have hindered the assembly of a complete 3 A data set.

机译：结晶和结构的确定重组体人载脂蛋白-ⅰ(apo -ⅰ),高密度的主要蛋白质成分脂蛋白,是描述。结晶,残留44 - 243的本地apo -ⅰ(apoδ(1)-ⅰ),非常类似于完好无损本机apo -ⅰ的脂质结合的能力,被纳入高密度脂蛋白和激活lecithin-cholesterol酰基转移酶。1.0 - -1.4 M柠檬酸钠在太空中pH值6.5 - -7.5集团P2(1) 2(1) 2(1),晶胞参数= 97.47, b = 113.87, c = 196.19(晶体形式我)。晶体表现出不同寻常的衍射峰值强度和轴向灭绝在4晶体的背景下讨论结构。晶体衍射同步加速器辐射3决议。crystal-to-crystal变化阻碍了组装一个完整的数据集。

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《Acta crystallographica.Section D. Biological crystallography》 |1999年第12期|2013-2021|共9页
作者
Borhani DW; Brouillette CG; Engler JA;
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作者单位

Department of Organic Chemistry, Southern Research Institute, Birmingham, AL 35205, USA. borhani@sri.org;

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原文格式 PDF
正文语种英语
中图分类
关键词
Human; Acyltransferases; CrystallographyElectrostaticsX-raysApolipoprotein A-ICrystallization;

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Human apolipoprotein A-I: structure determination and analysis of unusual diffraction characteristics.

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