STRUCTURE OF ACTIN BINDING DOMAIN OF CYCLASE ASSOCIATED PROTEIN

罗阿情结 晶体弱衍射至约4.5A 分辨率 采集140帧，每帧振荡0.5度。 曝光时间为30秒。 由于的各向异性 衍射图的数据仅在6A分辨率下才完整。 数据的整体完整性为86.2%。 数据的Rsym为 12%，整体冗余度为6。 总I/sigma为11.0（1.9 in 最后一个分辨率shell）。 这些数据目前用于分子 为了解决结构问题而进行的替换尝试。 PAF 乙酰水解酶突变体R22 K。 数据采集至1.9A 分辨率 数据的整体完整性为90%。 与 冗余度为5.4时，在20 ~ 1.9A的分辨率范围内，Rsym为7%。 该结构处于晶体学细化的最后阶段。

Rhoa complex. The crystals diffracted weakly to about 4.5A resolution. 140 frames were collected with oscillation of 0.5deg per frame and 30 seconds of exposure time. Due to the anisomorphism of the diffraction pattern the data are complete only to 6A resolution. The overall completeness of the data is 86.2%. Rsym for the data is 12% with the overall redundancy of 6. Overall I/sigma is 11.0 (1.9 in the last resolution shell). The data is currently used in molecular replacement attempts in order to solve the structure. PAF Acetylhydrolase mutant R22K. The data were collected to 1.9A resolution. The overall completeness of the data is 90%. With the redundancy of 5.4 the Rsym is 7% in resolution range from 20A to 1.9A. The structure is in the final stages of crystallographic refinement.