STRUCTURE OF ACTIN BINDING DOMAIN OF CYCLASE ASSOCIATED PROTEIN

Yeshiva University, New York NY

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Abstract

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.