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Space-Grown Protein Crystals Are More Useful for Structure Determination

Authors

  • JOSEPH D. NG

    Corresponding author
    1. Laboratory for Structural Biology and the Department of Biological Sciences, University of Alabama in Huntsville, Huntsville, Alabama, USA
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Address for correspondence: Joseph D. Ng, Laboratory for Structural Biology and the Department of Biological Sciences, University of Alabama in Huntsville, Huntsville, AL 35899, USA. Voice: 256-824-3715; fax: 256-824-3204; NgJ@email.uah.edu.

Abstract

Abstract: The usefulness of X-ray data derived from space-grown protein crystals for calculating a more accurate structure is reviewed here for three model proteins. These include the plant sweetening protein, thaumatin, from Thaumatococcus daniellii; the aspartyl-tRNA synthetase from Thermus thermophilus; and pea lectin from Pisum sativum. In all three cases, X-ray diffraction data collected from protein crystals obtained under reduced gravity lead to better defined initial electron density maps, facilitating model building and improved crystallographic statistics. With thaumatin, the phasing power of the anomalous scattering atom, sulfur, is used to determine protein crystal quality in terms of its usefulness for ab initio structure determination. Thaumatin crystals grown under microgravity provided improved phasing statistics compared to those of Earth-grown crystals. Consequently, generating a de novo protein model of higher quality was facilitated using X-ray diffraction data from space-grown crystals. This lends evidence to the possibility that a microgravity environment can favor protein crystal growth and, subsequently, be more useful for structure determination.

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