Research

Structural genomics of human proteins – target selection and generation of a public catalogue of expression clones

Konrad Büssow^1,2 , Christoph Scheich^1,2 , Volker Sievert^1,2 , Ulrich Harttig^1,4,5 , Jörg Schultz^3,8 , Bernd Simon³ , Peer Bork³ , Hans Lehrach^1,2 and Udo Heinemann^1,6,7

¹  Protein Structure Factory, Heubnerweg 6, 14059 Berlin, Germany

²  Max-Planck-Institut für Molekulare Genetik, Ihnestr. 73, 14195 Berlin, Germany

³  EMBL Heidelberg, Meyerhofstr. 1, 69117 Heidelberg, Germany

⁴  RZPD German Resource Center for Genome Research GmbH, Heubnerweg 6, 14059 Berlin, Germany

⁵  DIFE, Arthur-Scheunert-Allee 114–116, 14558 Nuthetal, Germany

⁶  Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Str. 10, 13092 Berlin, Germany

⁷  Institut für Chemie/Kristallographie, Freie Universität, Takustr. 6, 14195 Berlin, Germany

⁸  Department of Bioinformatics, University of Würzburg, Biocenter, Am Hubland, 97074 Würzburg, Germany

author email corresponding author email

Microbial Cell Factories 2005, 4:21doi:10.1186/1475-2859-4-21

Published:	5 July 2005

Abstract

Background

The availability of suitable recombinant protein is still a major bottleneck in protein structure analysis. The Protein Structure Factory, part of the international structural genomics initiative, targets human proteins for structure determination. It has implemented high throughput procedures for all steps from cloning to structure calculation. This article describes the selection of human target proteins for structure analysis, our high throughput cloning strategy, and the expression of human proteins in Escherichia coli host cells.

Results and Conclusion

Protein expression and sequence data of 1414 E. coli expression clones representing 537 different proteins are presented. 139 human proteins (18%) could be expressed and purified in soluble form and with the expected size. All E. coli expression clones are publicly available to facilitate further functional characterisation of this set of human proteins.