MACCHESS CONSORTIUM FOR LARGE MACROMOLECULAR STRUCTURES: HERPES VIRUS

青霉菌胃蛋白酶（EC 3.2.23.X）是一种天冬氨酸蛋白酶 来自真菌青霉菌 为了准备数据 收集在CHESS，晶体生长的天然酶和 其与两种环状膦酸酯抑制剂的络合物， 甲基[环-7 [（2R）-（（N-缬氨酰基） 氨基）-2-（羟基-（1S）-1-甲氧羰基-2-苯基-乙氧基）氧膦 (PP6)和甲基 环[（2S）-2-[[（1R）-1-（N-（L-N-（3-甲基丁酰基）缬氨酰基-L-缬氨酰基）氨基）- （PP7）。 膦酸盐抑制剂作为过渡的模拟物 在良好的衬底的分裂状态。 环化 抑制剂降低了它的灵活性，降低了熵成本， 与酶结合。 在国际象棋，晶体被转移到 母液溶液含有增加量的 冷冻保护剂，甘油。 最终溶液含有20%甘油， 40%饱和硫酸铵和100 mM乙酸钠，pH 4.6。 五个晶体的数据，一个天然的，两个复合体， 在100 K下用波长为0.919的X射线收集
关于ADSC F1站的Quantum-4 CCD探测器。 原始数据经过处理 至0.95
：针对143710个独特反射测量了415771个数据 （Rmerge = 6.8%），88.1%完成。 每一颗水晶的数据 复合物处理至0.90
分辨率 对于PP6，614135 测量由174924个独特的反射（Rmerge = 4.2%）进行， 89.7%完成;对于PP7，对156276个样本进行了459707次测量 唯一反射（Rmerge = 5.3%），完成80.1%至0.90
.的 目前正在根据这些数据完善三个模型。 的 晶体学残差为11.2%，为11.8 PP7复合物为11.0%。

Penicillopepsin (EC 3.2.23.X) is an aspartic proteinase isolated from the fungus Penicillium janthinellum. In preparation for the data collection at CHESS, crystals were grown of the native enzyme and of its complexes with two cyclic phosphonate inhibitors, methyl[cyclo-7[(2R)-((N-valyl) amino)-2-(hydroxyl-(1S)-1-methyoxycarbonyl-2-phenyl-ethoxy)phosphinyloxy (PP6) and methyl cyclo[(2S)-2-[[(1R)-1-(N-(L-N-(3-methylbutanoyl)valyl-L-aspartyl)amino)- (PP7). The phosphonate inhibitors act as mimics of the transition state in the cleavage of good substrates. Cyclization of the inhibitor reduces its flexibility and lowers the entropic cost of binding to the enzyme. At CHESS, crystals were transferred to solutions of the mother liquor containing increasing amounts of the cryoprotectant, glycerol. The final solution contained 20% glycerol, 40% saturated ammonium sulfate and 100 mM sodium acetate at pH 4.6. Data from five crystals, one of the native and two of each complex, were collected at 100 K with X-rays of wavelength 0.919
on the ADSC Quantum-4 CCD detector at station F1. The native data were processed to 0.95
: 415771 data were measured for 143710 unique reflections (Rmerge = 6.8%), 88.1% complete. The data from one crystal of each complex were processed to 0.90
resolution. For PP6, 614135 measurements were made of 174924 unique reflections (Rmerge = 4.2%), 89.7% complete; for PP7, 459707 measurements were made of 156276 unique reflections (Rmerge = 5.3%), 80.1% complete to 0.90
. The three models are currently being refined against these data. The crystallographic residuals are 11.2% for the native, 11.8% for the PP6 complex and 11.0% for the PP7 complex.