Crystal structure of Hen Egg White Lysozyme in complex with I3C

IF 2.2 4区生物学

Acta Crystallographica Section D: Biological Crystallography Pub Date : 2019-07-01 DOI:10.2210/PDB6PBB/PDB

J. Truong, S. Panjikar, L. Shearwin-Whyatt, J. Bruning, K. Shearwin

引用次数: 0

Abstract

Two commonly encountered bottlenecks in the structure determination of a protein by X-ray crystallography are screening for conditions that give high-quality crystals and, in the case of novel structures, finding derivatization conditions for experimental phasing. In this study, the phasing molecule 5-amino-2,4,6-triiodoisophthalic acid (I3C) was added to a random microseed matrix screen to generate high-quality crystals derivatized with I3C in a single optimization experiment. I3C, often referred to as the magic triangle, contains an aromatic ring scaffold with three bound I atoms. This approach was applied to efficiently phase the structures of hen egg-white lysozyme and the N-terminal domain of the Orf11 protein from Staphylococcus phage P68 (Orf11 NTD) using SAD phasing. The structure of Orf11 NTD suggests that it may play a role as a virion-associated lysin or endolysin.

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蛋清溶菌酶与I3C配合物的晶体结构

通过x射线晶体学确定蛋白质结构时，经常遇到的两个瓶颈是筛选提供高质量晶体的条件，以及在新结构的情况下，寻找衍生化条件进行实验分相。在本研究中，将相位分子5-氨基-2,4,6-三碘二苯二甲酸(I3C)添加到随机微种子基质筛选中，通过单次优化实验生成了高质量的I3C衍生晶体。I3C，通常被称为神奇三角，包含一个芳香环支架，有三个束缚的I原子。该方法应用于葡萄球菌噬菌体P68 (Orf11 NTD)中蛋清溶菌酶结构和Orf11蛋白n端结构域的SAD分相。Orf11 NTD的结构表明它可能作为病毒粒子相关的溶酶或内溶酶发挥作用。

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.