作者: Thomas Earnest , Eric Fauman , Charles S. Craik , Robert Stroud
关键词:
摘要: The structure of a rat trypsin mutant [S195C] at temperature 120 K has been refined to crystallographic R factor 17.4% between 12.0 and 1.59 A is compared with the D102N 295 K. reduction in unit cell dimensions going from room low accompanied by decrease molecular surface area radius gyration. overall remains similar that temperature. attainable resolution appears be improved due fall off intensities [reduction factor]. This decreases uncertainty atomic positions allows localization more protein atoms solvent molecules map. largest differences two models occur residues higher than average factors. Several features can localized region map are not seen These include several water as well an interstitial sulfate ion benzamidine molecules.