Work

Preliminary neutron and ultrahigh-resolution X-ray diffraction studies of the aspartic proteinase endothiapepsin cocrystallized with agem-diol inhibitor

Year: 2007

Type: article

Abstract: 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 A) 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.

Source: Acta Crystallographica Section F Structural Biology and Crystallization Communications

DOI: 10.1107/s1744309107061283

Authors: Han-Fang Tuan, Peter Erskine, Paul Langan, Jon Cooper, Leighton Coates

Institutions: Oak Ridge National Laboratory, Spallation Neutron Source, University College London, Los Alamos National Laboratory, University of Toledo

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Award: Computational Tools for Neutron Protein Crystallography