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Protein Engineering, Vol. 12, No. 5, 371-373, May 1999
© 1999 Oxford University Press

Short Communication

Proteolytic cleavage of Gram-positive ß recombinase is required for crystallization

Peter Orth, Petra Jekow, Juan C. Alonso1 and Winfried Hinrichs2

Institut für Kristallographie, Freie Universität Berlin, Takustraße 6, 14195 Berlin, Germany and 1 Departamento de Biotecnología Microbiana, Centro Nacional de Biotecnología, C.S.I.C., Campus de la Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain

ß Recombinase, a DNA resolvase-invertase, catalyzes in the presence of a chromatin-associated protein such as Hbsu, DNA resolution or DNA inversion on supercoiled substrates containing two directly or inversely oriented target (six) sites. Single crystals of the ß recombinase from plasmid pSM19035 were obtained using the vapor diffusion technique with ammonium phosphate as the precipitating agent. The crystals diffracted X-rays to a maximum resolution of 2.5Å. Due to proteolytic degradation during the crystallization experiment, the crystals contain only the N-terminal catalytic domain of ß recombinase corresponding to about 60% of the molecular mass of the initially assayed native protein. The proteolytic removal of the C-terminal DNA-binding domain demonstrated that protein modification can be essential to provide material suitable for X-ray analysis.

Keywords: catalytic domain/protein crystallization/proteolytic fragment/resolvase-invertase

2 To whom correspondence should be addressed


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