Walsh M A, Dementieva I, Evans G, Sanishvili R, Joachimiak A
Building 202, Argonne National Laboratory, 9700 South Cass Avenue, Argonne, IL 60439, USA.
Acta Crystallogr D Biol Crystallogr. 1999 Jun;55(Pt 6):1168-73. doi: 10.1107/s0907444999003698.
Multiwavelength anomalous diffraction data were measured in 23 min from a 16 kDa selenomethionyl substituted protein, producing experimental phases to 2.25 A resolution. The data were collected on a mosaic 3 x 3 charge-coupled device using undulator radiation from the Structural Biology Center 19ID beamline at the Argonne National Laboratory's Advanced Photon Source. The phases were independently obtained semiautomatically by two crystallographic program suites, CCP4 and CNS. The quality and speed of this data acquisition exemplify the opportunities at third-generation synchrotron sources for high-throughput protein crystal structure determination.
在23分钟内从一个16 kDa的硒代甲硫氨酸取代蛋白上收集了多波长反常衍射数据，得到了分辨率为2.25 Å的实验相位。数据是在阿贡国家实验室先进光子源的结构生物学中心19ID束线使用波荡器辐射，在一个3×3的镶嵌电荷耦合器件上收集的。相位由两个晶体学程序包CCP4和CNS独立半自动获得。这种数据采集的质量和速度体现了第三代同步辐射源在高通量蛋白质晶体结构测定方面的机遇。
