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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The role of CAPS buffer in expanding the crystallization space of the nucleotide-binding domain of the ABC transporter haemolysin B from Escherichia coli.
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The role of CAPS buffer in expanding the crystallization space of the nucleotide-binding domain of the ABC transporter haemolysin B from Escherichia coli.

机译：在扩大帽缓冲的作用结晶nucleotide-binding的空间域的ABC转运蛋白溶血素B大肠杆菌。

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摘要

Nucleotide-binding domains (NBDs), which are roughly 27 kDa in size, are conserved components of the large family of ABC (ATP-binding cassette) transporters, which includes importers and exporters. NBDs, or ABC-ATPases, supply energy for the translocation of a vast range of substrates across biological membranes. Despite their hydrophilic sequence, many NBDs readily associate in some way with membranes but demonstrate extreme instability in solution upon separation from the complete transporter. Conditions that stabilized the purified ABC domain of the Escherichia coli haemolysin A (HlyA) transporter were developed. This allowed the screening of unlimited crystallization conditions in the presence of different substrates, the performance of reproducible functional assays and the protection of 50 mg ml(-1) protein from precipitation on ice for months. As a result, it became possible to obtain crystals of HlyB-NBD in the presence of ADP and ATP that were suitable for X-ray analysis. Although the focus ofthese investigations was placed on HlyB-NBD, the strategy described here can be directly transferred to other proteins that display instability in solution.
机译：Nucleotide-binding域(nbd)大约27 kDa的大小,是守恒的组件大家庭的ABC(磷酸腺苷磁带)转运蛋白,包括进口商和出口商。易位的一个巨大的范围的在生物膜基质。他们的亲水序列,许多nbd容易将以某种方式与膜演示解决方案极端不稳定分离从完整的运输车。稳定了纯化ABC的条件域的大肠杆菌溶血素(HlyA)运输发达。无限的结晶的筛查在不同的条件基板,可再生的性能功能分析和50毫克的保护毫升(1)蛋白质沉淀在冰上个月。晶体的HlyB-NBD ADP和的存在ATP是适合x射线分析。尽管这些调查重点放在HlyB-NBD,这里描述的策略可以直接转移到其他蛋白质显示不稳定的解决方案。

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