Hajdu J, Machin P A, Campbell J W, Greenhough T J, Clifton I J, Zurek S, Gover S, Johnson L N, Elder M
Nature. 1987;329(6135):178-81. doi: 10.1038/329178a0.
Attempts to use X-ray crystallography to extract three-dimensional information on transient phenomena in crystals have been hampered primarily by long data collection times. Here we report on the first difference Fourier map obtained from Laue diffraction photographs of a protein crystal, glycogen phosphorylase b. Data collection time was 3 s using the high-intensity white X-radiation generated on the wiggler magnet of the Daresbury Synchrotron Radiation Source (SRS), but data acquisition in the millisecond-submillisecond range is possible. The method presented here uses a simple difference technique and was designed to analyse structural changes relative to a known starting structure. The combination of this approach with cine techniques allows the recording of three-dimensional motion pictures at atomic resolution and opens up new areas in structural biology and chemistry.
利用X射线晶体学来获取晶体中瞬态现象的三维信息的尝试，主要受到较长数据收集时间的阻碍。在此，我们报告了从蛋白质晶体糖原磷酸化酶b的劳厄衍射照片中获得的首张差值傅里叶图。使用达累斯伯里同步辐射源（SRS）的摆动磁铁产生的高强度白色X射线，数据收集时间为3秒，但在毫秒至亚毫秒范围内进行数据采集也是可行的。这里介绍的方法采用了一种简单的差值技术，旨在分析相对于已知起始结构的结构变化。这种方法与电影技术相结合，能够以原子分辨率记录三维动态图像，并为结构生物学和化学开辟了新的领域。
