Native sulfur/chlorine SAD phasing for serial femtosecond crystallography.

Native sulfur/chlorine SAD phasing for serial femtosecond crystallography.
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DOI:
10.1107/s139900471501857x
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发表时间:
2015-12-01
期刊:
Acta crystallographica. Section D, Biological crystallography
影响因子:
--
通讯作者:
Sugahara M
Sugahara M
中科院分区:
其他
文献类型:
--
作者:
Nakane T;Song C;Suzuki M;Nango E;Kobayashi J;Masuda T;Inoue S;Mizohata E;Nakatsu T;Tanaka T;Tanaka R;Shimamura T;Tono K;Joti Y;Kameshima T;Hatsui T;Yabashi M;Nureki O;Iwata S;Sugahara M

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硫 SAD 定相有助于使用来自自由电子激光器的飞秒 X 射线通过串行飞秒晶体学确定多种天然蛋白质的结构。串行飞秒晶体学 (SFX) 可以在辐射损伤最小的情况下确定结构。然而,在 SFX 中对原生晶体进行定相并不常见。在这里,成功地证明了利用 1.77 Å 波长下硫和氯的异常信号,通过单波长异常衍射 (SAD) 测定天然溶菌酶的结构。这种硫 SAD 方法可应用于多种蛋白质,这将改善天然晶体结构的测定。
Sulfur SAD phasing facilitates the structure determination of diverse native proteins using femtosecond X-rays from free-electron lasers via serial femtosecond crystallography. Serial femtosecond crystallography (SFX) allows structures to be determined with minimal radiation damage. However, phasing native crystals in SFX is not very common. Here, the structure determination of native lysozyme from single-wavelength anomalous diffraction (SAD) by utilizing the anomalous signal of sulfur and chlorine at a wavelength of 1.77 Å is successfully demonstrated. This sulfur SAD method can be applied to a wide range of proteins, which will improve the determination of native crystal structures.