Linac Coherent Light Source, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.
Science. 2012 Jul 20;337(6092):362-4. doi: 10.1126/science.1217737. Epub 2012 May 31.
Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.
蛋白质和其他生物大分子的结构测定在过去需要生长出高质量的晶体，这些晶体要足够大，以便有效地进行 X 射线衍射，同时还要能抵御辐射损伤。我们采用了使用自由电子激光（XFEL）的连续飞秒结晶学（SFX）技术，从具有良好特征的模型蛋白溶菌酶的微晶体（小于 1 微米×1 微米×3 微米）中获得了高分辨率的结构信息。与同步加速器数据的一致性证明了 SFX 对于分析大量难以结晶的分子的结构具有直接的相关性。
