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Facilities and methods for the high-throughput crystal structural analysis of human proteins

Official URL:https://doi.org/10.1021/ar010129t
PubMed:View item in PubMed
Creators Name:Heinemann, U. and Buessow, K. and Mueller, U. and Umbach, P.
Journal Title:Accounts of Chemical Research
Journal Abbreviation:Acc Chem Res
Volume:36
Number:3
Page Range:157-163
Date:March 2003
Keywords:Expressed Sequence Tags, Genomics, Human Genome Project, Molecular Cloning, Tertiary Protein Structure, Recombinant Fusion Proteins, X-Ray Crystallography
Abstract:Facilities and methods for the high-throughput crystal structure analysis of human proteins are described as recently established in the Protein Structure Factory, a Berlin-area structural genomics project. Genes encoding human proteins are expressed in either recombinant Escherichia coli or yeast (Saccharomyces cerevisiae or Pichia pastoris). To facilitate and standardize protein purification, the target proteins are produced with various tags for affinity chromatography. For high-throughput crystallization, a robotic station is being set up that has the capacity to handle 960 000 experiments simultaneously. The resulting protein crystals will be subjected to X-ray diffraction experiments at the third-generation synchrotron storage ring BESSY where protein crystallography beamlines are currently under construction. The Protein Structure Factory's strategy for high-throughput production and structure analysis of human proteins is evaluated based on first results.
ISSN:0001-4842
Publisher:Ameri Chemical Soc (U.S.A.)
Item Type:Review

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