PROTEIN SINGLE-CRYSTAL DIFFRACTION WITH 5 ANGSTROM SYNCHROTRON X-RAYSAT THE SULFUR K-ABSORPTION EDGE

Citation
Ms. Lehmann et al., PROTEIN SINGLE-CRYSTAL DIFFRACTION WITH 5 ANGSTROM SYNCHROTRON X-RAYSAT THE SULFUR K-ABSORPTION EDGE, Acta crystallographica. Section D, Biological crystallography, 49, 1993, pp. 308-310
Citations number
14
ISSN journal
09074449
Volume
49
Year of publication
1993
Part
2
Pages
308 - 310
Database
ISI
SICI code
0907-4449(1993)49:<308:PSDW5A>2.0.ZU;2-Z
Abstract
Sulfur atoms, an integral part of many proteins, are possible candidat es for anomalous scattering in phase determination by multiple-wavelen gth methods. The main difficulty encountered is that a wavelength of a bout 5 angstrom is required to obtain a large anomalous signal from th ese atoms, leading to very large absorption effects. Initial experimen ts have been carried out using a synchrotron X-ray source, evacuated b eam 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.