Ontology highlight
ABSTRACT:
SUBMITTER: Rhys NH
PROVIDER: S-EPMC3004261 | biostudies-literature | 2011 Jan
REPOSITORIES: biostudies-literature
Rhys Natasha H NH Wang Ming Chuan MC Jowitt Thomas A TA Helliwell John R JR Grossmann J Günter JG Baldock Clair C
Journal of synchrotron radiation 20101105 1
The low-resolution structure of α-crustacyanin has been determined to 30 Å resolution using negative-stain electron microscopy (EM) with single-particle averaging. The protein, which is an assembly of eight β-crustacyanin dimers, appears asymmetrical and rather open in layout. A model was built to the EM map using the X-ray crystallographic structure of β-crustacyanin guided by PISA interface analyses. The model has a theoretical sedimentation coefficient that matches well with the experimentall ...[more]