Engineering of recombinant crystallization chaperones.

Engineering of recombinant crystallization chaperones.
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DOI:
10.1016/j.sbi.2009.04.008
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发表时间:
2009-08
影响因子:
6.8
通讯作者:
Koide, Shohei
Koide, Shohei
中科院分区:
生物学2区
文献类型:
--
作者:
Koide, Shohei

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衍射质量晶体的制备仍然是大分子x射线晶体学的主要瓶颈。结晶分子伴侣是一种辅助蛋白,如单克隆抗体片段,其结合并增加目标靶分子的结晶概率。这样的分子伴侣减少构象异质性,掩盖适得其反的表面,同时延伸表面倾向于形成晶体接触,并提供定相信息。使用重组技术产生的结晶分子伴侣已经作为上级替代物出现,其增加通量并消除与通过动物免疫和杂交瘤技术产生抗体相关的固有限制。
The preparation of diffraction quality crystals remains the major bottleneck in macromolecular x-ray crystallography. A crystallization chaperone is an auxiliary protein, such as fragments of monoclonal antibodies, that binds to and increases the crystallization probability of a target molecule of interest. Such chaperones reduce conformational heterogeneity, mask counterproductive surfaces while extending surfaces predisposed to forming crystal contacts, and provide phasing information. Crystallization chaperones generated using recombinant technologies have emerged as superior alternatives that increase the throughput and eliminate inherent limitations associated with antibody production by animal immunization and the hybridoma technology.
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