Applying X-Ray Topography and Diffractometry to Improve Protein Crystal Growth

Published

February 21, 2001

Author(s)

David R. Black, L Arnowitz, David T. Gallagher

Abstract

In order to obtain adequate diffraction data to determine the structure of the protein of interest, crystal quality is important. Although in this context there may be no single concise definition of quality, it must involve adequate size, singleness (ideally the crystal comprises a single molecular lattice), and several diffraction criteria. Diffraction is key to the crystal's usefulness: resolution and mosaicity are the two best estimators of diffraction quality, yet each is difficult to measure objectively. In the final analysis, every protein presents its own challenges to obtaining well-diffracting crystals, and there is probably no single definition of quality that will do for all cases. This paper describes the growth of ribonuclease S crystals under otherwise similar conditions in space and on earth and the techniques used to compare the crystals that were obtained.

Proceedings Title

Proceedings of Space Technology and Applications International Forum

Conference Dates

January 30-February 3, 2000

Conference Title

International Forum on Space Technology and Applications

Pub Type

Conferences

Keywords

diffraction, protein, ribonuclease, topography

Citation

Black, D. , Arnowitz, L. and Gallagher, D. (2001), Applying X-Ray Topography and Diffractometry to Improve Protein Crystal Growth, Proceedings of Space Technology and Applications International Forum (Accessed December 12, 2024)