Cryocrystallography of biological macromolecules: a generally applicable method
- 1 February 1988
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta crystallographica Section B, Structural science, crystal engineering and materials
- Vol. 44 (1) , 22-26
- https://doi.org/10.1107/s0108768187008632
Abstract
Methods have been developed that allow facile X-ray data collection for biological macromolecules at cryogenic (near liquid N2) temperatures. The crystals are first transferred from their mother liquor to a hydrocarbon environment, then mounted with a standard glass fiber (no capillary), and flash cooled in situ with a cold nitrogen stream on the diffraction apparatus. This approach prevents freezing of the solvent in the crystals, so that they maintain their crystallographic integrity. Significant improvement of resolution can result from the cryogenic data collection, and radiation damage in the cooled crystals is greatly reduced, or eliminated, for the duration of data collection.This publication has 4 references indexed in Scilit:
- Structure of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1984
- Conformational substates in a protein: structure and dynamics of metmyoglobin at 80 K.Proceedings of the National Academy of Sciences, 1982
- Structure of a B-DNA dodecamer at 16 K.Proceedings of the National Academy of Sciences, 1982
- Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphurNature, 1981