摘要
Wang's phase filtering procedure has been applied to the structure study of trichosan- thin crystals belonging to space group C2.The MIR phases at 3 resolution have been improved with the accumulative phase shift of 31.8°and the figure of merit has been improved from 0.54 to 0.84.The resulted electron density map at 3 resolution has been much improved with a higher ratio of the electron density of the protein to the noise in the solvent region.The minimap has been interpreted more reasonably than the previous maps,giving the overall course of the polypeptide chain substantially the same as previously reported except for containing more secondary structure and a few short segments traced differently.The first 85 C_α atoms of the polypeptide chain are located in about the same positions as determined previously with an exception of a short segment but the amino acid residues after that shift along the chain with a maximum shift of about 15 residues. The electron density of side chains agrees better with the primary structure.The conformation and the three-dimensional structure as well as the major heavy-atom binding sites for the two molecules in an asymmetric unit are substantially the same.The structure of trichosanthin shows more similarity to ricin A chain than that reported previously.
Wang's phase filtering procedure has been applied to the structure study of trichosan- thin crystals belonging to space group C2.The MIR phases at 3 resolution have been improved with the accumulative phase shift of 31.8°and the figure of merit has been improved from 0.54 to 0.84.The resulted electron density map at 3 resolution has been much improved with a higher ratio of the electron density of the protein to the noise in the solvent region.The minimap has been interpreted more reasonably than the previous maps,giving the overall course of the polypeptide chain substantially the same as previously reported except for containing more secondary structure and a few short segments traced differently.The first 85 C_α atoms of the polypeptide chain are located in about the same positions as determined previously with an exception of a short segment but the amino acid residues after that shift along the chain with a maximum shift of about 15 residues. The electron density of side chains agrees better with the primary structure.The conformation and the three-dimensional structure as well as the major heavy-atom binding sites for the two molecules in an asymmetric unit are substantially the same.The structure of trichosanthin shows more similarity to ricin A chain than that reported previously.
