STAFF PRIORITY TIME VERY HIGH RESOLUTION DATA FOR PHOSPHATE BINDING PROTEIN

在1.7E分辨率下，磷酸结合蛋白的结构为 1990年解决并出版(Luecke&Quiocho，自然347,402-406)。 使用最近安装的MAR扫描仪的2Q扩展，请访问 光束线7-1我们已收集到1.02东经的超高分辨率数据 对于来自一个冷冻天然和一个冷冻的磷酸盐结合蛋白 单点突变(T141D)突变。我们正在提炼过程中 数据使用SHELXL程序(谢尔德里克，Gvttingen)。首字母 FO-FC图显示了许多氢原子在 活动站点是预期的。我们希望能够解决这个问题 结合的无机磷酸盐的质子化状态。磷酸盐是 被12个氢键束缚。在8E以内没有溶剂分子 完全隔离的磷酸盐阴离子。当前的R因子 所有数据到1.02E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%.