X-ray crystallographic studies of the middle part of the human synaptonemal complex protein 1 coiled-coil domain

Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1131-4. doi: 10.1107/S2053230X15012728. Epub 2015 Aug 25.

Abstract

The synaptonemal complex is a meiosis-specific complex structure formed at the synapse of homologous chromosomes to hold them together during meiosis. Synaptonemal complex protein 1 (SYCP1) is one of the components of the syneptonemal complex. In this study, the short form of the coiled-coil domain of SYCP1 was overexpressed in Escherichia coli with an engineered C-terminal His tag. The short form of the coiled-coil domain of SYCP1 was then purified to homogeneity and crystallized at 293 K. X-ray diffraction data were collected to a resolution of 3.0 Å from a crystal belonging to space group I4, with unit-cell parameters a = 41.95, b = 41.95, c = 318.78 Å. The asymmetric unit was estimated to contain two molecules.

Keywords: SYCP1; coiled-coil domain; crystallization; meiosis; syneptonemal complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatography, Gel
  • Crystallization
  • Crystallography, X-Ray
  • DNA-Binding Proteins
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / isolation & purification
  • Protein Structure, Tertiary

Substances

  • DNA-Binding Proteins
  • Nuclear Proteins
  • SYCP1 protein, human