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AFM visualization of clathrin triskelia under fluid and in air |
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| Authors: | Svetlana Kotova Paul D Smith Ralph Nossal Albert J Jin |
| Institution: | a Laboratory of Bioengineering and Physical Science, National Institute of Biomedical Imaging and Bioengineering, National Institutes of Health, DHHS, Bethesda, MD 20892, United States b Department of Biochemistry, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, United States c Laboratory of Integrative and Medical Biophysics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, DHHS, Bethesda, MD 20892, United States |
| Abstract: | Atomic force microscopy (AFM) is used to characterize the structure and interactions of clathrin triskelia. Time sequence images of individual, wet triskelia resting on mica surfaces clearly demonstrate conformational fluctuations of the triskelia. AFM of dried samples yields images having nanometric resolution comparable to that obtainable by electron microscopy of shadowed samples. Increased numbers of triskelion dimers and assembly intermediates, as well as structures having dimensions similar to those of clathrin cages, are observed when the triskelia were immersed in a low salt, low pH buffer. These entities have been quantified by AFM protein volume computation.Structured summaryMINT-7299119, MINT-7299136:Clathrin (uniprotkb:P49951) and Clathrin (uniprotkb:P49951) bind (MI:0407) by atomic force microscopy (MI:0872) |
| Keywords: | Endocytosis Clathrin triskelion Biological AFM Macromolecular assembly Molecular flexibility |
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