Open AccessPreliminary neutron and ultrahigh‐resolution X‐ray diffraction studies of the aspartic proteinase endothiapepsin cocrystallized with a gem ‐diol inhibitor
Author(s) -
Tuan HanFang,
Erskine Peter,
Langan Paul,
Cooper Jon,
Coates Leighton
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107061283
Subject(s) - protonation , neutron diffraction , crystallography , x ray , resolution (logic) , chemistry , diffraction , x ray crystallography , solvent , materials science , stereochemistry , physics , crystal structure , computer science , organic chemistry , nuclear physics , optics , artificial intelligence , ion
Endothiapepsin has been cocrystallized with the gem ‐diol inhibitor PD‐135,040 in a low solvent‐content (39%) unit cell, which is unprecedented for this enzyme–inhibitor complex and enables ultrahigh‐resolution (1.0 Å) X‐ray diffraction data to be collected. This atomic resolution X‐ray data set will be used to deduce the protonation states of the catalytic aspartate residues. A room‐temperature neutron data set has also been collected for joint refinement with a room‐temperature X‐ray data set in order to locate the H/D atoms at the active site.