Improvements in lysozyme protein crystal perfection through microgravity growth.
Improvements in lysozyme protein crystal perfection through microgravity growth.
复制标题
通过微重力生长改善溶菌酶蛋白质晶体的完美性。
DOI：
--
复制
发表时间：
1995
期刊：
影响因子：
--
通讯作者：
K. Schroer
中科院分区：
文献类型：
--
作者：
E. Snell;S. Weisgerber;J. Helliwell;K. Hölzer;K. Schroer
微重力为蛋白质结晶提供了一个没有对流和沉淀的环境。我们研究了微重力条件对蛋白质晶体完善的影响。用于 X 射线衍射研究的晶体质量由许多因素表征，即尺寸、镶嵌性和分辨率极限。通过使用四方溶菌酶晶体作为测试案例，我们表明，在两次独立的航天飞机任务中晶体生长，镶嵌性比地球生长的地面对照值提高了三到四倍。这些微重力生长的蛋白质晶体本质上是完美的衍射光栅。因此，各个 X 射线衍射反射的峰与背景的增强程度与镶嵌性的降低类似。这为改进弱反射（例如在高衍射分辨率下发生的弱反射）的测量提供了特别重要的机会。这些微重力结果为所有未来微重力和基于地球的蛋白质晶体学程序设定了基准。
Microgravity offers an environment for protein crystallization where there is an absence of convection and sedimentation. We have investigated the effect of microgravity conditions on the perfection of protein crystals. The quality of crystals for X-ray diffraction studies is characterized by a number of factors, namely size, mosaicity and the resolution limit. By using tetragonal lysozyme crystals as a test case we show, with crystal growth in two separate Space Shuttle missions, that the mosaicity is improved by a factor of three to four over earth-grown ground control values. These microgravity-grown protein crystals are then essentially perfect diffraction gratings. As a result the peak to background of individual X-ray diffraction reflections is enhanced by a similar factor to the reduction in the mosaicity. This then offers a particularly important opportunity for improving the measurement of weak reflections such as occur at high diffraction resolution. These microgravity results set a benchmark for all future microgravity and earth-based protein crystallography procedures.