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PDBsum entry 3cx2
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Contractile protein
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PDB id
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3cx2
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References listed in PDB file
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Key reference
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Title
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An investigation into the protonation states of the c1 domain of cardiac myosin-Binding protein c.
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Authors
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S.J.Fisher,
J.R.Helliwell,
S.Khurshid,
L.Govada,
C.Redwood,
J.M.Squire,
N.E.Chayen.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2008,
64,
658-664.
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PubMed id
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Abstract
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Myosin-binding protein C (MyBP-C) is a myofibril-associated protein found in
cardiac and skeletal muscle. The cardiac isoform (cMyBP-C) is subject to
reversible phosphorylation and the surface-charge state of the protein is of
keen interest with regard to understanding the inter-protein interactions that
are implicated in its function. Diffraction data from the C1 domain of cMyBP-C
were extended to 1.30 A resolution, where the <I/sigma(I)> of the
diffraction data crosses 2.0, using intense synchrotron radiation. The
protonation-state determinations were not above 2sigma (the best was 1.81sigma)
and therefore an extrapolation is given, based on 100% data completeness and the
average DPI, that a 3sigma determination could be possible if X-ray data could
be measured to 1.02 A resolution. This might be possible via improved
crystallization or multiple sample evaluation, e.g. using robotics or a yet more
intense/collimated X-ray beam or combinations thereof. An alternative would be
neutron protein crystallography at 2 A resolution, where it is estimated that
for the unit-cell volume of the cMyBP-C C1 domain crystal a crystal volume of
0.10 mm3 would be needed with fully deuterated protein on LADI III. These
efforts would optimally be combined in a joint X-ray and neutron model
refinement.
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