SYNCHROTRON CRYSTALLOGRAPHY OF PROTEINS AT BEAMLINE X 9B

束线 X 9B 上蛋白质的同步加速器晶体学

• 批准号: 6120423
• 负责人: ZBIGNIEW DAUTER
• 金额: --
• 依托单位: ALBERT EINSTEIN COLLEGE OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 1998
• 资助国家: 美国
• 起止时间: 1998-09-30 至 1999-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6120423
• 关键词: biological products; biomedical resource; enzymes; proteins; spectrometry

Frozen TE2-SeMet crystals diffracted to ~2 A. Fluorescence scan has accurately determined the wavelengths for data collection. Three data sets have been collected from one seleno-methionine labeled crystal at 2.5A resolution at selected wavelengths. The exposure time was 45 seconds/frame and with 1 degree oscillations. The data are of very good quality with internal R-factors ranging from 4.3% to 4.8% and the overall completeness is 99.7%. Preliminary scaling results suggest that the signal should be strong enough to solve the structure using Se atoms as the anomalous scatterers. Experiments using direct methods as well as the Patterson function are carried out to find the positions of the Se atoms and calculate the phases.

冷冻的TE 2-SeMet晶体衍射至~2 A。荧光扫描 已经准确地确定了数据收集的波长。 三 数据集已收集从一个硒蛋氨酸标记 晶体在2.5A分辨率在选定的波长。 曝光时间 是45秒/帧并且具有1度振荡。 数据是 质量非常好，内部R因子范围为4.3%至4.8% 总体完成率为99.7%。 初步缩放结果 我认为信号应该足够强， 使用Se原子作为异常散射体。 实验使用直接 方法以及帕特森函数进行，以找到 Se原子的位置并计算相。