Hedman B, Hodgson K O, Helliwell J R, Liddington R, Papiz M Z
Proc Natl Acad Sci U S A. 1985 Nov;82(22):7604-7. doi: 10.1073/pnas.82.22.7604.
By using ultra-high-flux synchrotron x-radiation from a wiggler source, good Laue diffraction data have been obtained from protein microcrystals of size 30 X 35 X 10 microns3, mounted wet in glass capillaries. At the flux level of 10(13)-10(14) photons per sec/mm2, the radiation damage is still low enough to allow a large survey of reciprocal space for a microcrystal and a complete survey for a normal-sized protein crystal. The development of sources for ultra-high-intensity synchrotron radiation is thus an important improvement in the technique for determination of structure through protein crystallography as well as in other cases where crystal size is often a limiting factor.
通过使用来自摆动器源的超高通量同步加速器X射线，已从尺寸为30×35×10微米³、湿态安装在玻璃毛细管中的蛋白质微晶获得了良好的劳厄衍射数据。在每秒每平方毫米10¹³ - 10¹⁴个光子的通量水平下，辐射损伤仍然足够低，能够对微晶的倒易空间进行大范围探测，并对正常尺寸的蛋白质晶体进行完整探测。因此，超高强度同步加速器辐射源的发展是蛋白质晶体学结构测定技术以及晶体尺寸常常成为限制因素的其他情况中的一项重要改进。
