An investigation into the protonation states of the C1 domain of cardiac myosin-binding protein C

S J Fisher, J R Helliwell, S Khurshid, L Govada, C Redwood, JM Squire, N E Chayen

Research output: Contribution to journalArticle (Academic Journal)peer-review

Abstract

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 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.
Translated title of the contributionAn investigation into the protonation states of the C1 domain of cardiac myosin-binding protein C
Original languageEnglish
Pages (from-to)658 - 664
Number of pages7
JournalActa Crystallographica Section D: Biological Crystallography
Volume64
DOIs
Publication statusPublished - Jun 2008

Fingerprint Dive into the research topics of 'An investigation into the protonation states of the C1 domain of cardiac myosin-binding protein C'. Together they form a unique fingerprint.

Cite this