Purification, crystallization, and preliminary X-Ray diffraction analysis of the carbapenem-hydrolyzing class A beta-lactamase Sme-1 from Serratia marcescens.

@article{Sougakoff1996PurificationCA,
  title={Purification, crystallization, and preliminary X-Ray diffraction analysis of the carbapenem-hydrolyzing class A beta-lactamase Sme-1 from Serratia marcescens.},
  author={Wladimir Sougakoff and Vincent Jarlier and Jean Delettr{\'e} and N Colloc'h and G L'hermite and Patrice L. Nordmann and Thierry Naas},
  journal={Journal of structural biology},
  year={1996},
  volume={116 2},
  pages={313-6}
}
The carbapenem-hydrolyzing class A beta-lactamase Sme-1 from Serratia marcescens S6 was expressed in Escherichia coli and purified by ion-exchange chromatography and gel filtration. Crystals of the purified enzyme were obtained by the hanging drop vapor diffusion method using polyethylene glycol 4000 as precipitant. The crystals belong to the monoclinic space group P21 with unit cell parameters a = 81.48 A, b = 51.76 A, c = 71.81 A, alpha = gamma = 90 degrees, and beta = 118.71 degrees. There… CONTINUE READING

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