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Control of strain in subgrains of protein crystals by the introduction of grown‐in dislocations
Acta Crystallographica Section D ( IF 2.6 ) Pub Date : 2021-05-05 , DOI: 10.1107/s2059798321001820
Haruhiko Koizumi 1 , Satoshi Uda 2 , Ryo Suzuki 3 , Masaru Tachibana 3 , Kenichi Kojima 4 , Katsuo Tsukamoto 5 , Izumi Yoshizaki 6 , Seijiro Fukuyama 7 , Yoshihisa Suzuki 8
Affiliation  

It is important to reveal the exact cause of poor diffractivity in protein crystals in order to determine the accurate structure of protein molecules. It is shown that there is a large amount of local strain in subgrains of glucose isomerase crystals even though the overall crystal quality is rather high, as shown by clear equal‐thickness fringes in X‐ray topography. Thus, a large stress is exerted on the subgrains of protein crystals, which could significantly lower the resistance of the crystals to radiation damage. It is also demonstrated that this local strain can be reduced through the introduction of dislocations in the crystal. This suggests that the introduction of dislocations in protein crystals can be effective in enhancing the crystal quality of subgrains of protein crystals. By exploiting this effect, the radiation damage in subgrains could be decreased, leading to the collection of X‐ray diffraction data sets with high diffractivity.

中文翻译:

通过引入位错控制蛋白质晶体亚晶的应变

为了确定蛋白质分子的准确结构,揭示蛋白质晶体衍射性差的确切原因很重要。结果表明,尽管整体晶体质量相当高,但葡萄糖异构酶晶体的亚晶粒中存在大量局部应变,如 X 射线形貌中清晰的等厚条纹所示。因此,在蛋白质晶体的亚晶粒上施加了很大的应力,这可能会显着降低晶体对辐射损伤的抵抗力。还证明可以通过在晶体中引入位错来减少这种局部应变。这表明在蛋白质晶体中引入位错可以有效提高蛋白质晶体亚晶粒的晶体质量。通过利用这种效应,
更新日期:2021-05-06
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