MACCHESS CONSORTIUM FOR LARGE MACROMOLECULAR STRUCTURES: HERPES VIRUS

青霉蛋白酶(EC 3.2.23.X)是一种分离的天冬氨酸蛋白酶 从真菌简氏青霉中提取。为数据做准备 收集国际象棋时，晶体生长的天然酶和 其与两种环状膦酸类抑制剂的络合物， 甲基[环-7][(2R)-((N-钒) Amino)-2-(hydroxyl-(1S)-1-methyoxycarbonyl-2-phenyl-ethoxy)phosphinyloxy (PP6)和甲基 Cyclo[(2S)-2-[[(1R)-1-(N-(L-N-(3-methylbutanoyl)valyl-L-aspartyl)amino)- (PP7)。磷酸盐类抑制剂是这种转变的模拟物。 在好的底物的解理中的状态。的环化作用 抑制剂降低了其灵活性，并降低了信息量成本 与酶结合。在国际象棋比赛中，水晶被转移到 母液的溶液中含有越来越多的 低温保护剂，甘油。最终的溶液含有20%的甘油， 40%饱和硫酸铵和100 mM乙酸钠，pH 4.6。 来自五个晶体的数据，一个是原生晶体，两个是复合体， 在100K下用波长0.919的X射线收集关于ADSC F1站的量子4号ccd探测器。对原始数据进行处理 至0.95：415771个数据针对143710个独特的反射进行了测量 (重新合并=6.8%)，完成88.1%。来自每个晶体的数据 复合体被加工到0.90决议。对于pp6,614135 测量了174924个独特的反射(RMerge=4.2%)， 89.7%完成；对于购买力平价7,459707次测量是156276次 独特反射(重新合并=5.3%)，完成80.1%至0.90。这个 根据这些数据，目前正在改进三个模型。这个 晶体残留量为11.2%，PP6为11.8% 复合体和PP7复合体占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.