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Protein Engineering, Vol. 12, No. 2, 151-153, February 1999
© 1999 Oxford University Press

Homogenization and crystallization of histidine ammonia-lyase by exchange of a surface cysteine residue

Torsten F. Schwede1, Mathias Bädeker1, Martin Langer2, Janos Rétey2 and Georg E. Schulz1,3

1 Institut für Organische Chemie und Biochemie, Albertstrasse 21,D-79104 Freiburg im Breisgau and 2 Institut für Organische Chemie, Lehrstuhl Biochemie der Universität, Richard-Willstätter-Allee, D-76128 Karlsruhe, Germany

Histidase (histidine ammonia-lyase, EC 4.3.1.3) from Pseudomonas putida was expressed in Escherichia coli and purified. In the absence of thiols the tetrameric enzyme gave rise to undefined aggregates and suitable crystals could not be obtained. The solvent accessibility along the chain was predicted from the amino acid sequence. Among the seven cysteines, only one was labeled as `solvent-exposed'. The exchange of this cysteine to alanine abolished all undefined aggregations and yielded readily crystals diffracting to 1.8 Å resolution.

Keywords: disulfide engineering/Ellman's reaction/histidine ammonia-lyase/unspecific aggregation/X-ray crystallography

3 To whom correspondence should be addressed. E-mail: schulz{at}bio5.chemie.uni-freiburg.de


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