Escherichia coli MltA: MAD phasing and refinement of a tetartohedrally twinned protein crystal structure (vol D61, pg 613, 2005)

IF 2.2 4区生物学 Acta Crystallographica Section D: Biological Crystallography Pub Date : 2005-08-01 DOI:10.1107/S0907444905013533

T. Barends, R. D. Jong, K. Straaten, A. Thunnissen, B. Dijkstra

引用次数: 0

Abstract

Crystals were grown of a mutant form of the bacterial cell-wall maintenance protein MltA that diffracted to 2.15 A resolution. When phasing with molecular replacement using the native structure failed, selenium MAD was used to obtain initial phases. However, after MAD phasing the crystals were found to be tetartohedrally twinned, hampering correct space-group determination and refinement. A refinement protocol was designed to take tetartohedral twinning into account and was successfully applied to refine the structure. The refinement protocol is described and the reasons for the failure of molecular replacement and the success of MAD are discussed in terms of the effects of the tetartohedral twinning.

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大肠杆菌MltA:四面体双生蛋白晶体结构的MAD相位和细化(vol D61, pg 613, 2005)

晶体由细菌细胞壁维持蛋白MltA的突变体生长而成，其衍射分辨率为2.15 a。当使用天然结构的分子置换相失败时，使用硒MAD获得初始相。然而，经过MAD相位后，发现晶体是四面孪晶，阻碍了正确的空间群测定和细化。设计了一种考虑四面体孪生的改进方案，并成功地应用于改进结构。叙述了分子置换失败的原因，并从四面体孪晶的影响方面讨论了分子置换成功的原因。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Acta Crystallographica Section D: Biological Crystallography 生物-晶体学

自引率

13.60%

发文量

审稿时长

3 months

期刊介绍： Acta Crystallographica Section D welcomes the submission of articles covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules or the methods used to determine them. Reports on new structures of biological importance may address the smallest macromolecules to the largest complex molecular machines. These structures may have been determined using any structural biology technique including crystallography, NMR, cryoEM and/or other techniques. The key criterion is that such articles must present significant new insights into biological, chemical or medical sciences. The inclusion of complementary data that support the conclusions drawn from the structural studies (such as binding studies, mass spectrometry, enzyme assays, or analysis of mutants or other modified forms of biological macromolecule) is encouraged. Methods articles may include new approaches to any aspect of biological structure determination or structure analysis but will only be accepted where they focus on new methods that are demonstrated to be of general applicability and importance to structural biology. Articles describing particularly difficult problems in structural biology are also welcomed, if the analysis would provide useful insights to others facing similar problems.

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