- Abstract:
-
Elucidation of the accurate subunit stoichiometry of oligomeric membrane proteins is fraught with complexities. The interpretations of chemical cross-linking, analytical ultracentrifugation, gel filtration, and low-resolution electron microscopy studies are often ambiguous. Staphylococcal alpha-hemolysin (alpha HL), a homooligomeric toxin that forms channels in cell membranes, was believed to possess six subunits arranged around a sixfold axis of symmetry. Here, we report that analysis of x-r...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1073/pnas.91.26.12828
-
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- Journal:
- Proceedings of the National Academy of Sciences of the United States of America
- Volume:
- 91
- Issue:
- 26
- Pages:
- 12828-12831
- Publication date:
- 1994-12-05
- DOI:
- EISSN:
-
1091-6490
- ISSN:
-
0027-8424
- URN:
-
uuid:d0847fbb-c9e6-441a-b5c3-eb734c75ef22
- Source identifiers:
-
52441
- Local pid:
- pubs:52441
- Copyright date:
- 1994
Journal article
Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore.
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