On the reproducibility of protein crystal structures: five atomic resolution structures of trypsin.

ABSTRACT: Structural studies of proteins usually rely on a model obtained from one crystal. By investigating the details of this model, crystallographers seek to obtain insight into the function of the macromolecule. It is therefore important to know which details of a protein structure are reproducible or to what extent they might differ. To address this question, the high-resolution structures of five crystals of bovine trypsin obtained under analogous conditions were compared. Global parameters and structural details were investigated. All of the models were of similar quality and the pairwise merged intensities had large correlation coefficients. The C(α) and backbone atoms of the structures superposed very well. The occupancy of ligands in regions of low thermal motion was reproducible, whereas

SUBMITTER: Liebschner D 

PROVIDER: S-EPMC3727327 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature