STAFF PRIORITY TIME VERY HIGH RESOLUTION DATA FOR PHOSPHATE BINDING PROTEIN

磷酸结合蛋白在1.7E分辨率下的结构是 在1990年解决并发表（Luecke和Quiocho，Nature 347，402-406）。 随着最近安装的MAR扫描仪的2 q扩展， 光束线7-1，我们已经收集了超高分辨率的数据，以1.02 E 分别从一个冷冻的天然和一个冷冻的 单位点突变体（T141 D）突变体。 我们正在提炼 用SHELXL程序（Sheldrick，Gvttingen）处理数据。 初始 Fo-Fc图显示在其中许多氢原子在分子中的位置处的峰。 活性位点是预期。 我们希望能够解决 结合的无机磷酸盐的质子化状态。 述磷酸盐是 由12个氢键组成。 在8 E内没有溶剂分子 完全隔离的磷酸根阴离子。 当前R因素 在1.02 E时，所有数据的平均值为14%，RFREE为18.7%。

The structure of phosphate-binding protein at 1.7 E resolution was solved and published in 1990 (Luecke & Quiocho, Nature 347, 402-406). With the recently installed 2q extension of the MAR scanner at beamline 7-1 we have collected ultra-high resolution data to 1.02 E for phosphate-binding protein from one frozen native and one frozen single-site mutant (T141D) mutant. We are in the process of refining the data with the program SHELXL (Sheldrick, Gvttingen). Initial Fo-Fc maps show peaks at the positions where many of the hydrogens in the active site are expected. We hope to be able to resolve the protonation state of the bound inorganic phosphate. The phosphate is bound by 12 hydrogen bonds. There are no solvent molecules within 8 E of the completely sequestered phosphate anion. The current R-factor is 14% for all data to 1.02 E, the RFREE is 18.7%.