Scanning transmission electron microscopy study of the molecular mass of amphipol/cytochrome b6f complexes.
The composition and mass of complexes between Chlamydomonas reinhardtii cytochrome b6f and low molecular mass amphipathic polymers ('amphipols') have been studied using biochemical analysis and scanning transmission electron microscopy at liquid helium temperature (cryo-STEM). Cytochrome b6f was trapped by amphipols either under its native 14-meric state or as a delipidated, lighter form. A good consistency was observed between the masses of either form calculated from their biochemical composition and those determined by cryo-STEM. These data show that association with amphipols preserved the original original state of the protein in detergent solution. Complexation with amphipols appears to facilitate preparation of the samples and mass determination by cryo-STEM as compared to conventional solubilization with detergents.
CNRS-UMR 7615, Paris, France.
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Tribet
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Mills
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Haider
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Popot
D000818:Animals; D002498:Centrifugation; D016825:Chlamydomonas reinhardtii / Q000201:enzymology; D003573:Cytochrome b Group / Q000737:chemistry*; D045346:Cytochrome b6f Complex; D003902:Detergents; D005615:Freezing; D017348:Microscopy, Electron, Scanning Transmission / Q000379:methods*; D008970:Molecular Weight; D011108:Polymers / Q000737:chemistry*; D013501:Surface-Active Agents / Q000737:chemistry*
D003573:Cytochrome b Group; D003902:Detergents; D011108:Polymers; D013501:Surface-Active Agents; D045346:Cytochrome b6f Complex