Ontology highlight
ABSTRACT:
SUBMITTER: Larson SB
PROVIDER: S-EPMC2650472 | biostudies-literature | 2009 Mar
REPOSITORIES: biostudies-literature
Larson Steven B SB Day John S JS Nguyen Chieugiang C Cudney Robert R McPherson Alexander A
Acta crystallographica. Section F, Structural biology and crystallization communications 20090212 Pt 3
Proteinase K, a subtilisin-like fungal protease, was crystallized from a cocktail of small molecules containing digalacturonic acid (DGA). The crystal structure was determined to 1.32 A resolution and refined to an R factor of 0.158. The final model contained, beside the protein, two calcium ions, 379 water molecules, a molecule of DGA and a partially occupied HEPES molecule. The DGA molecule has one sugar moiety disposed exactly on a crystallographic twofold axis; the second ring was not observ ...[more]