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| Content Provider | Springer Nature Link |
|---|---|
| Author | Straus, S. K. Scott, W. R. P. Symmons, M. F. Marvin, D. A. |
| Copyright Year | 2007 |
| Abstract | The filamentous bacteriophage (Inovirus) strain Ff (fd, f1, M13) is widely used in molecular biophysics as a simple model system. A low resolution molecular model of the fd protein coat has been reported, derived from iterative helical real space reconstruction of cryo-electron micrographs (cryoEM). This model is significantly different from the model previously derived from X-ray fibre diffraction and solid-state NMR. We show that the cryoEM model agrees neither with solid-state NMR data nor with X-ray fibre diffraction data of fd, and has some puzzling structural features, for instance nanometre holes through the protein coat. We refine the cryoEM model against the X-ray data, and find that the model after refinement closely approximates the model derived directly from X-ray fibre diffraction and solid-state NMR data. We suggest possible reasons for the differences between the models derived from cryoEM and X-ray diffraction. |
| Starting Page | 521 |
| Ending Page | 527 |
| Page Count | 7 |
| File Format | |
| ISSN | 01757571 |
| Journal | European Biophysics Journal |
| Volume Number | 37 |
| Issue Number | 4 |
| e-ISSN | 14321017 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2007-10-18 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | α-Helix Fibre diffraction Solid-state NMR Cryo-electron microscopy Helical reconstruction Neurobiology Animal Physiology Plant Physiology Biochemistry Cell Biology Biophysics/Biomedical Physics |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Biophysics |
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