Purification, crystallization and identification by X-ray analysis of a prostate kallikrein from horse seminal plasma

Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1180-3. doi: 10.1107/s0907444901009805. Epub 2001 Jul 23.

Abstract

The purification, crystallization and identification by X-ray diffraction analysis of a horse kallikrein is reported. The protein was purified from horse seminal plasma. Crystals belong to space group C2 and the structure was solved by the MIRAS method, with two heavy-atom derivatives of mercury and platinum. X-ray diffraction data to 1.42 A resolution were collected at the ESRF synchrotron-radiation source.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Horses
  • Kallikreins / chemistry*
  • Kallikreins / isolation & purification
  • Male
  • Models, Molecular
  • Molecular Sequence Data
  • Prostate / chemistry*
  • Protein Conformation
  • Semen / chemistry*
  • Sequence Homology, Amino Acid

Substances

  • Kallikreins