Crystallography without crystals I: the common-line method for assembling a 3D intensity volume from single-particle scattering
| dc.creator | Shneerson, V. L. | |
| dc.creator | Ourmazd, A. | |
| dc.creator | Saldin, D. K. | |
| dc.date | 2007-10-14 | |
| dc.date.accessioned | 2026-07-07T08:36:12Z | |
| dc.date.available | 2026-07-07T08:36:12Z | |
| dc.description | We demonstrate that a common-line method can assemble a 3D oversampled diffracted intensity distribution suitable for high-resolution structure solution from a set of measured 2D diffraction patterns, as proposed in experiments with an X-ray free electron laser (XFEL) (Neutze {\it et al.}, 2000). Even for a flat Ewald sphere, we show how the ambiguities due to Friedel's Law may be overcome. The method breaks down for photon counts below about 10 per detector pixel, almost 3 orders of magnitude higher than expected for scattering by a 500 kDa protein with an XFEL beam focused to a 0.1 micron diameter spot. Even if 10**3 orientationally similar diffraction patterns could be identified and added to reach the requisite photon count per pixel, the need for about 10**6 orientational classes for high-resolution structure determination suggests that about ~ 10**9 diffraction patterns must be recorded. Assuming pulse and read-out rates of 100 Hz, such measurements would require ~ 10**7 seconds, i.e. several months of continuous beam time. | |
| dc.description | 27 pages, 9 figures | |
| dc.identifier | https://arxiv.org/abs/0710.2561 | |
| dc.identifier | http://arxiv.org/abs/0710.2561 | |
| dc.identifier.uri | http://salesiana.dossiersoluciones.com/handle/123456789/139985 | |
| dc.subject | Biomolecules | |
| dc.title | Crystallography without crystals I: the common-line method for assembling a 3D intensity volume from single-particle scattering | |
| dc.type | text |