ArticleActa crystallographica. Section F, Structural biology and crystallization communications2007
Preliminary neutron and ultrahigh-resolution X-ray diffraction studies of the aspartic proteinase endothiapepsin cocrystallized with a gem-diol inhibitor.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Hemoglobin redux: combining neutron and X-ray diffraction with mass spectrometry to analyse the quaternary state of oxidized hemoglobins.Acta crystallographica. Section D, Biological crystallography · 2010Article
- Macromolecular neutron crystallography at the Protein Crystallography Station (PCS).Acta crystallographica. Section D, Biological crystallography · 2010Article
- Preliminary neutron and X-ray crystallographic studies of equine cyanomethemoglobin.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Engineering an improved crystal contact across a solvent-mediated interface of human fibroblast growth factor 1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Neutron crystallography: opportunities, challenges, and limitations.Current opinion in structural biology · 2008Review
- The catalytic mechanism of an aspartic proteinase explored with neutron and X-ray diffraction.Journal of the American Chemical Society · 2008Article
- Protein structures by spallation neutron crystallography.Journal of synchrotron radiation · 2008Article
- Preliminary time-of-flight neutron diffraction study of human deoxyhemoglobin.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
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.
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