An optimal exposure strategy for cryoprotected virus crystals with lattice constants greater than 1000 Å
- Scripps
Studies of icosahedral virus capsids provide insights into the function of supramolecular machines. Virus capsid crystals have exceptionally large unit cells; as a result, they diffract weakly compared with protein crystals. HK97 is a dsDNA lambda-like bacteriophage whose 13 MDa capsid expands from 550 {angstrom} to 650 {angstrom} with large subunit conformational changes during virus maturation. The HK97 penultimate maturation intermediate was crystallized in a tetragonal unit cell that has lattice constants of 1010 {angstrom} x 1010 {angstrom} x 730 {angstrom}. The crystals could be cryoprotected, but diffracted to a modest resolution of 5 {angstrom} at a bending-magnet beamline. When these crystals were optimally exposed with two orders-of-magnitude more photons from a new insertion-device beamline, data extending to better than 3.8 {angstrom} resolution were obtained. Here, the strategies to collect and process such data are described. These strategies can be adapted for other crystals with large unit cells and for microcrystals.
- Research Organization:
- Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 1006576
- Journal Information:
- J. Synchrotron Rad., Journal Name: J. Synchrotron Rad. Journal Issue: (3) ; 05, 2008 Vol. 15; ISSN 0909-0495; ISSN JSYRES
- Country of Publication:
- United States
- Language:
- ENGLISH
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