Crystallization and preliminary X-ray diffraction analysis of boar seminal plasma spermadhesin PSP-I/PSP-II, a heterodimer of two CUB domains

FEBS Lett. 1996 Mar 11;382(1-2):15-7. doi: 10.1016/0014-5793(96)00133-0.

Abstract

Boar spermadhesin PSP-I/PSP-II (M(r) 29 000-30 000), a non-covalent heterodimer of two CUB domains, was crystallized in two crystal forms. Complete diffraction data sets for hexagonal (space group P6(1,5)22) and trigonal (space group P3(1,2)21) crystals have been collected up to 2.9 and 2.5 angstrom resolution, respectively. Cell constants of the hexagonal and trigonal crystal forms are a=b=87.2 angstrom, c=152.4 angstrom, and a=b=96.2 angstrom, c=70.8 angstrom, respectively. The calculated packing parameters (Vm) are 2.8 and 3.2 angstrom(3)/DA for the hexagonal and trigonal crystal forms, respectively, indicating that, in both cases, the asymmetric unit is constituted by one PSP-I/PSP-II heterodimer. This paper reports the first crystals of a protein built up by a CUB domain architecture.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Glycoproteins / chemistry*
  • Male
  • Molecular Sequence Data
  • Protein Conformation
  • Semen / chemistry*
  • Seminal Vesicle Secretory Proteins*
  • Sequence Analysis
  • Swine

Substances

  • Glycoproteins
  • Seminal Vesicle Secretory Proteins
  • seminal vesicle secretory protein II, porcine
  • seminal vesicle secretory protein 109, porcine