Farber G K, Machin P, Almo S C, Petsko G A, Hajdu J
Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.
Proc Natl Acad Sci U S A. 1988 Jan;85(1):112-5. doi: 10.1073/pnas.85.1.112.
The Laue method (stationary crystal, polychromatic x-rays) was used to collect native and heavy-atom-derivative data on crystals of xylose isomerase (EC 5.3.1.5). These data were used to find the heavy-atom positions. The positions found by use of Laue data are the same as those found by use of monochromatic data collected on a diffractometer. These results confirm that Laue diffraction data sets, which can be obtained on a millisecond time scale, can be used to locate small molecules bound to protein active sites. The successful determination of heavy-atom positions also indicates that x-ray crystallographic data collected by the Laue method can be used to solve protein structures.
劳厄法(固定晶体,多色X射线)被用于收集木糖异构酶(EC 5.3.1.5)晶体的天然数据和重原子衍生物数据。这些数据被用于确定重原子的位置。使用劳厄数据找到的位置与使用衍射仪收集的单色数据找到的位置相同。这些结果证实,可在毫秒时间尺度上获得的劳厄衍射数据集可用于定位与蛋白质活性位点结合的小分子。重原子位置的成功确定还表明,通过劳厄法收集的X射线晶体学数据可用于解析蛋白质结构。