In this section
@article{Govada:2023:10.1007/s10974-023-09648-2,
author = {Govada, L and Chayen, NE},
doi = {10.1007/s10974-023-09648-2},
journal = {Journal of Muscle Research and Cell Motility},
pages = {209--215},
title = {Crystallisation and characterisation of muscle proteins: a mini-review},
url = {http://dx.doi.org/10.1007/s10974-023-09648-2},
volume = {44},
year = {2023}
}
TY - JOUR
AB - The techniques of X-ray protein crystallography, NMR and high-resolution cryo-electron microscopy have all been used to determine the high-resolution structure of proteins. The most-commonly used method, however, remains X-ray crystallography but it does rely heavily on the production of suitable crystals. Indeed, the production of diffraction quality crystals remains the rate-limiting step for most protein systems. This mini-review highlights the crystallisation trials that used existing and newly developed crystallisation methods on two muscle protein targets - the actin binding domain (ABD) of α-actinin and the C0-C1 domain of human cardiac myosin binding protein C (cMyBP-C). Furthermore, using heterogenous nucleating agents the crystallisation of the C1 domain of cMyBP-C was successfully achieved in house along with preliminary actin binding studies using electron microscopy and co-sedimentation assays .
AU - Govada,L
AU - Chayen,NE
DO - 10.1007/s10974-023-09648-2
EP - 215
PY - 2023///
SN - 0142-4319
SP - 209
TI - Crystallisation and characterisation of muscle proteins: a mini-review
T2 - Journal of Muscle Research and Cell Motility
UR - http://dx.doi.org/10.1007/s10974-023-09648-2
UR - https://www.ncbi.nlm.nih.gov/pubmed/37133758
VL - 44
ER -