Importance of Determination of Crystal Quality in Protein Crystals when Performing High-Resolution Structural Analysis
Importance of Determination of Crystal Quality in Protein Crystals when Performing High-Resolution Structural Analysis
复制标题
进行高分辨率结构分析时确定蛋白质晶体晶体质量的重要性
DOI:
10.1021/acs.cgd.6b00457
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发表时间:
2016
影响因子:
3.8
通讯作者:
Kenichi
中科院分区:
文献类型:
--
作者:
Koizumi;Haruhiko Suzuki;Ryo Tachibana;Masaru Tsukamoto;Katsuo Yoshizaki;Izumi Fukuyama;Seijiro Suzuki;Yoshihisa Uda;Satoshi Kojima;Kenichi
We show that the extinction effect explained by the dynamical theory of diffraction must be considered even in the case of protein crystals. Equal-thickness fringes, which are attributed to the Pendellösung effect, were clearly observed in the region of a tapered glucose isomerase crystal with wedge-like edges using X-ray topography carried out with a beam of monochromatic synchrotron radiation. This indicates that the perfection of this glucose isomerase crystal is high enough to produce this dynamical theory-related effect: this surely leads to difficulty in the collection of accurate integrated intensities of diffraction spots for X-ray structural analysis. Therefore, it is important to determine whether the crystal quality of a protein crystal under analysis is adequate to obtain accurate three-dimensional structures of protein molecules for X-ray structural analyses. We show that X-ray diffraction rocking-curve measurements can provide clues for this determination.