Improvements in lysozyme protein crystal perfection through microgravity growth

E. H. Snell, S. Weisgerber, J. R. Helliwell, E. Weckert, K. Hölzer, K. Schroer
  • Acta Crystallographica Section D Biological Crystallography, November 1995, International Union of Crystallography
  • DOI: 10.1107/s0907444995012170

Microgravity crystal growth improved long range crystal order

Photo by SpaceX on Unsplash

Photo by SpaceX on Unsplash

What is it about?

Some protein crystals grown in microgravity have shown dramatic improvements in the data that can be obtained from them. This paper showed that mosaicity was improved by a factor of three to four. Mosaicity can be thought of as how well aligned the domains making up the crystal are. The microgravity grown sample was much better ordered.

Why is it important?

The experiment was technically challenging - the quality of the microgravity grown crystals approached the limits of measurement. Until recently this quality could not be exploited without sophisticated measurement approaches. With new beamlines, faster detectors, and continuous rotation methods it is now technically possible to exploit enhancements in physical quality (long-range order) to improve knowledge of the short-range structure (resolution).

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http://dx.doi.org/10.1107/s0907444995012170

The following have contributed to this page: Professor John Richard Helliwell and Dr Edward H Snell