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Title
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Preliminary neutron and ultrahigh-resolution X-ray diffraction studies of the aspartic proteinase endothiapepsin cocrystallized with a gem-diol inhibitor.
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Authors
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H.F.Tuan,
P.Erskine,
P.Langan,
J.Cooper,
L.Coates.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2007,
63,
1080-1083.
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PubMed id
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Abstract
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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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