Published in

International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 12(63), p. 1080-1083, 2007

DOI: 10.1107/s1744309107061283

Links

Tools

Export citation

Search in Google Scholar

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

Journal article published in 2007 by Han-Fang Tuan, Peter Erskine, Paul Langan ORCID, Jon Cooper, Leighton Coates
This paper is available in a repository.
This paper is available in a repository.

Full text: Download

Green circle
Preprint: archiving allowed
Upload
Green circle
Postprint: archiving allowed
Upload
Green circle
Published version: archiving allowed
Upload
Policy details
Data provided by SHERPA/RoMEO

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.