Schmidt Andrea, Teeter Martha, Weckert Edgar, Lamzin Victor S
EMBL Hamburg, c/o DESY, Notkestrasse 85, D-22607 Hamburg, Germany.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt 4):424-8. doi: 10.1107/S1744309110052607. Epub 2011 Mar 24.
With the development of highly brilliant and extremely intense synchrotron X-ray sources, extreme high-resolution limits for biological samples are now becoming attainable. Here, a study is presented that sets the record in crystallographic resolution for a biological macromolecule. The structure of the small protein crambin was determined to 0.48 Å resolution on the PETRA II ring before its conversion to a dedicated synchrotron-radiation source. The results reveal a wealth of details in electron density and demonstrate the possibilities that are potentially offered by a high-energy source. The question now arises as to what the true limits are in terms of what can be seen at such high resolution. From what can be extrapolated from the results using crystals of crambin, this limit would be at approximately 0.40 Å, which approaches that for smaller compounds.
随着高亮度、极高强度的同步加速器X射线源的发展，现在生物样品的极高分辨率极限已变得可以实现。在此，介绍一项在生物大分子晶体学分辨率方面创下纪录的研究。在小蛋白胰凝乳蛋白酶抑制剂转变为专用同步辐射源之前，在PETRA II环上确定了其结构，分辨率达到0.48 Å。结果揭示了电子密度中的大量细节，并展示了高能源可能提供的可能性。现在出现的问题是，在如此高分辨率下能够看到的真实极限是什么。从使用胰凝乳蛋白酶抑制剂晶体的结果推断，这个极限大约在0.40 Å，这已接近较小化合物的极限。
