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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure determination of a novel protein by sulfur SAD using chromium radiation in combination with a new crystal-mounting method
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Structure determination of a novel protein by sulfur SAD using chromium radiation in combination with a new crystal-mounting method

机译：结构新颖的蛋白质的测定使用铬辐射硫悲伤结合一种新的crystal-mounting方法

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摘要

A novel and easy crystal-mounting technique was developed for the sulfur SAD method using Cr K alpha radiation (2.29 angstrom). Using this technique, the cryo-buffer and cryoloop around the protein crystal can be removed before data collection in order to eliminate their X-ray absorption. The superiority and reproducibility of the data sets with this mounting technique were demonstrated using tetragonal hen egg-white lysozyme crystals. The structure of a novel protein, PH1109, from Pyrococcus horikoshii OT3 was solved using this technique. At the wavelength of Cr K alpha radiation, the anomalous signal [|Delta F|// h| F|] of PH1109 is expected to be 1.72% as this protein of 144 residues includes four methionines and two cysteines. Sulfur SAD phasing was performed using SHELXD and SHELXE. In the case of the data set obtained using this novel crystal-mounting technique, 54.9% of all residues were built with side chains automatically by RESOLVE. On the other hand, only 16.0% were built with side chains for the data set collected using the standard cryoloop. These results indicated that this crystal-mounting technique was superior to the standard loop-mounting method for the measurement of small anomalous differences at longer wavelength and yielded better results in sulfur-substructure solution and initial phasing. The present study demonstrates that the sulfur SAD method with a chromium source becomes enhanced and more practical for macromolecular structure determination using the new crystal-mounting technique.
机译：小说,容易crystal-mounting技术使用Cr K为硫悲伤的方法开发阿尔法辐射(2.29埃)。技术,cryo-buffer cryoloop蛋白质晶体可以删除之前的数据为了消除他们的x射线集合吸收。数据集的安装技术演示了使用正方母鸡蛋白吗溶菌酶晶体。蛋白质、PH1109从海床horikoshii OT3解决了使用这种技术。Cr Kα辐射的波长反常信号(δh | | / / F | |) PH1109预计1.72%,这144残基的蛋白质包括四个蛋氨酸和两个半胱氨酸。使用SHELXD和硫悲伤分阶段进行SHELXE。利用这本小说crystal-mounting技术,54.9%的残留与侧链建成自动解决。16.0%是由侧链的数据使用标准cryoloop收集。结果表明,这种crystal-mounting技术优于标准loop-mounting小的测量方法较长波长和异常差异在sulfur-substructure产生更好的结果解决方案和初步定相。表明硫悲伤的方法铬源成为增强等等实际的大分子结构使用新的crystal-mounting决心技术。

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