title: Correlation between protein sequence similarity and crystallization reagents in the biological macromolecule crystallization database.
abstract: The protein structural entries grew far slower than the sequence entries. This is partly due to the bottleneck in obtaining diffraction quality protein crystals for structural determination using X-ray crystallography. The first step to achieve protein crystallization is to find out suitable chemical reagents. However, it is not an easy task. Exhausting trial and error tests of numerous combinations of different reagents mixed with the protein solution are usually necessary to screen out the pursuing crystallization conditions. Therefore, any attempts to help find suitable reagents for protein crystallization are helpful. In this paper, an analysis of the relationship between the protein sequence similarity and the crystallization reagents according to the information from the existing databases is presented. We extracted information of reagents and sequences from the Biological Macromolecule Crystallization Database (BMCD) and the Protein Data Bank (PDB) database, classified the proteins into different clusters according to the sequence similarity, and statistically analyzed the relationship between the sequence similarity and the crystallization reagents. The results showed that there is a pronounced positive correlation between them. Therefore, according to the correlation, prediction of feasible chemical reagents that are suitable to be used in crystallization screens for a specific protein is possible.
authors.affiliation: Institute of Special Environmental Biophysics, School of Life Sciences, Northwestern Polytechnical University, Xi'an 710072, Shaanxi, China.|Key Laboratory for Space Bioscience and Biotechnology, Northwestern Polytechnical University, Xi'an 710072, Shaanxi, China.
authors.forename: Hui-Meng
authors.initials: HM
authors.lastname: Lu
authors.affiliation: Institute of Special Environmental Biophysics, School of Life Sciences, Northwestern Polytechnical University, Xi'an 710072, Shaanxi, China.|Key Laboratory for Space Bioscience and Biotechnology, Northwestern Polytechnical University, Xi'an 710072, Shaanxi, China.
authors.forename: Da-Chuan
authors.initials: DC
authors.lastname: Yin
authors.affiliation: Institute of Special Environmental Biophysics, School of Life Sciences, Northwestern Polytechnical University, Xi'an 710072, Shaanxi, China.|Key Laboratory for Space Bioscience and Biotechnology, Northwestern Polytechnical University, Xi'an 710072, Shaanxi, China.
authors.forename: Yong-Ming
authors.initials: YM
authors.lastname: Liu
authors.affiliation: Institute of Special Environmental Biophysics, School of Life Sciences, Northwestern Polytechnical University, Xi'an 710072, Shaanxi, China.|Key Laboratory for Space Bioscience and Biotechnology, Northwestern Polytechnical University, Xi'an 710072, Shaanxi, China.
authors.forename: Wei-Hong
authors.initials: WH
authors.lastname: Guo
authors.affiliation: Institute of Special Environmental Biophysics, School of Life Sciences, Northwestern Polytechnical University, Xi'an 710072, Shaanxi, China.
authors.forename: Ren-Bin
authors.initials: RB
authors.lastname: Zhou
mesh_terms: D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D030562:Databases, Protein; D006801:Humans; D046912:Multiprotein Complexes / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*; D017385:Sequence Homology
chemical_list: D046912:Multiprotein Complexes; D011506:Proteins