Protein single-crystal diffraction with 5 Å synchrotron X-rays at the sulfur K-absorption edge
- 1 March 1993
- journal article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography
- Vol. 49 (2) , 308-310
- https://doi.org/10.1107/s0907444992011910
Abstract
. Sulfur atoms, an integral part of many proteins, are possible candidates for anomalous scattering in phase determination by multiple-wavelength methods. The main difficulty encountered is that a wavelength of about 5 A is required to obtain a large anomalous signal from these atoms, leading to very large absorption effects. Initial experiments have been carried out using a synchrotron X-ray source, evacuated beam tubes, a diffractometer inside a vacuum chamber, a special sample holder and a suitable scattering geometry. The results are encouraging, showing that Bragg reflections can be measured, and that changes in their intensities around the absorption edge are observable.Keywords
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