Deriving the ultrastructure of α-crustacyanin using lower-resolution structural and biophysical methods

Natasha H. Rhys, Ming Chuan Wang, Thomas A. Jowitt, John R. Helliwell, J. Günter Grossmann, Clair Baldock

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    Abstract

    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 experimentally derived value from sedimentation velocity analytical ultracentrifugation. Additionally, the EM model has similarities to models calculated independently by rigid-body modelling to small-angle X-ray scattering (SAXS) data and extracted in silico from the β-crustacyanin crystal lattice. Theoretical X-ray scattering from each of these models is in reasonable agreement with the experimental SAXS data and together suggest an overall design for the α-crustacyanin assembly.
    Original languageEnglish
    Pages (from-to)79-83
    Number of pages4
    JournalJournal of Synchrotron Radiation
    Volume18
    Issue number1
    DOIs
    Publication statusPublished - Jan 2011

    Keywords

    • α-crustacyanin
    • analytical ultracentrifugation
    • crystal packing of 1gka
    • EM
    • PISA
    • SAXS

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