HIGH RES XRAY DIFFRACTION DATA COLLECTION OF EUKARYOTIC TRANSCRIPTION FACTORS

从冷冻保护的（30%葡萄糖） 载脂蛋白A-I apo（143）A-I晶体（P212121，a = 97.47，B = 0.001） 113.87，c = 196.19 1997年7月13日在CHESS光束线A-1上进行的（100 K，70 0.5“振荡框架，60秒，130 mm探测器距离）。 数据 与CAMLM集成，与SCALA缩放，并进一步处理 CCP 4套件 这些数据完成57%到3.0  决议， Rsym为11.4%（3.2 3.0中为37.9  shell）。 这些数据 比我们在实验室里收集的要好得多， 用于求解4的结构  分辨率 然而，即使在100 K时， 这些晶体仍然对辐射损伤极其敏感， 衍射到3  我们使用的国际象棋光束线A-1上 该项目验证了这些载脂蛋白（（1 43）A-I） 晶体晶体的作用更好，4  分辨率 附加数据 计划在CHESS收集这些数据，以便 在3处细化  可以开始了。 我们也期待未来的数据 在CHESS从我们的低盐I222 apo（（143）A-I晶体收集 形式，以及我们正在研究的其他形式的载脂蛋白A-I晶体 laboratories.

Diffraction data were collected from a cryoprotected (30% glucose) apolipoprotein A-I apo ((1 43)A-I crystal (P212121, a = 97.47, b = 113.87, c = 196.19 ) at CHESS beamline A-1 on 13 July 1997 (100 K, 70 0.5' oscillation frames, 60 sec, 130 mm detector distance). The data were integrated with MOSFLM, scaled with SCALA, and further processed with the CCP4 suite. These data are 57% complete to 3.0  resolution, with an Rsym of 11.4% (37.9% in the 3.2 3.0  shell). These data are dramatically better than those that we collected in our laboratory and used to solve the structure at 4  resolution. Even at 100 K, however, these crystals remain extremely sensitive to radiation damage, diffracting to 3  for only 30 min. Our use of CHESS beamline A-1 on this project has validated the notion that these apo ((1 43)A-I crystals diffract to better that 4  resolution. Additional data collection at CHESS is planned to complete these data, so that refinement at 3  can commence. We also look forward to future data collection at CHESS from our low-salt I222 apo ((1 43)A-I crystal form, and crystals of other forms of apo A-I under study in our laboratories.