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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.

Original publication

DOI

10.1107/S0907444908008792

Type

Journal article

Journal

Acta Crystallogr D Biol Crystallogr

Publication Date

06/2008

Volume

64

Pages

658 - 664

Keywords

Aspartic Acid, Carrier Proteins, Crystallography, X-Ray, Glutamic Acid, Humans, Models, Molecular, Neutron Diffraction, Protein Structure, Tertiary, Protons, Recombinant Proteins, Static Electricity, Synchrotrons