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

Torsten Schwede | Zendy; Mathias Bädeker | Zendy; Martin Langer | Zendy; János Rétey | Zendy; Georg E. Schulz | Zendy

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

Author(s) -

Torsten Schwede,

Mathias Bädeker,

Martin Langer,

János Rétey,

Georg E. Schulz

Publication year - 1999

Publication title -

protein engineering design and selection

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.627

H-Index - 109

eISSN - 1741-0134

pISSN - 1741-0126

DOI - 10.1093/protein/12.2.151

Subject(s) - histidine , cysteine , chemistry , lyase , residue (chemistry) , crystallization , ammonia , alanine , pseudomonas putida , escherichia coli , solvent , amino acid , biochemistry , stereochemistry , enzyme , organic chemistry , gene

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 A resolution.

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