title: Correlation between protein sequence similarity and x-ray diffraction quality in the protein data bank.
abstract: As the most widely utilized technique to determine the 3-dimensional structure of protein molecules, X-ray crystallography can provide structure of the highest resolution among the developed techniques. The resolution obtained via X-ray crystallography is known to be influenced by many factors, such as the crystal quality, diffraction techniques, and X-ray sources, etc. In this paper, the authors found that the protein sequence could also be one of the factors. We extracted information of the resolution and the sequence of proteins from the Protein Data Bank (PDB), classified the proteins into different clusters according to the sequence similarity, and statistically analyzed the relationship between the sequence similarity and the best resolution obtained. The results showed that there was a pronounced correlation between the sequence similarity and the obtained resolution. These results indicate that protein structure itself is one variable that may affect resolution when X-ray crystallography is used.
authors.affiliation: Institute of Special Environmental Biophysics, Faculty of Life Sciences, Northwestern Polytechnical University, Xi'an 710072, Shaanxi, PR China.
authors.forename: Hui-Meng
authors.initials: HM
authors.lastname: Lu
authors.forename: Da-Chuan
authors.initials: DC
authors.lastname: Yin
authors.forename: Ya-Jing
authors.initials: YJ
authors.lastname: Ye
authors.forename: Hui-Min
authors.initials: HM
authors.lastname: Luo
authors.forename: Li-Qiang
authors.initials: LQ
authors.lastname: Geng
authors.forename: Hai-Sheng
authors.initials: HS
authors.lastname: Li
authors.forename: Wei-Hong
authors.initials: WH
authors.lastname: Guo
authors.forename: Peng
authors.initials: P
authors.lastname: Shang
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D030562:Databases, Protein; D017385:Sequence Homology