Applications of synchrotron radiation to protein crystallography: preliminary results.
- 1 January 1976
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 73 (1) , 128-132
- https://doi.org/10.1073/pnas.73.1.128
Abstract
X-ray diffraction photographs of protein single crystals have been obtained using synchrotron radiation produced by an electron-positron storage ring. The diffracted intensities observed with this unconventional source are a factor of at least 60 greater than those obtained with a sealed X-ray tube using the same crystal and instrumental parameters. Diffraction data were collected by the precession method to higher resolution and using smaller protein crystals than were possible with a conventional source. The crystal decay rate in the synchrotron beam for several proteins appears to be substantially less than that observed with Ni-filtered Cu radiation. The tunable nature of the source (which allows selective optimization of anomalous contributions to the scattering factors) and the low angular divergence of the beam make the source very useful for single crystal protein diffraction studies.Keywords
This publication has 1 reference indexed in Scilit:
- Crystallization of nerve growth factor from mouse submaxillary glands.Proceedings of the National Academy of Sciences, 1975