Crystallization and preliminary X-ray diffraction studies of an a1/alpha 2/DNA ternary complex

Proteins. 1995 Feb;21(2):161-4. doi: 10.1002/prot.340210210.

Abstract

Crystals have been obtained of a ternary complex containing the yeast a1/alpha 2 homeodomain heterodimer bound to a 21-base pair DNA site containing two 5' overhanging bases at each end. The crystals are grown from cobaltic hexamine and form in space group P6(1) or P6(5) with a = b = 133 A, c = 45.4 A. Crystals that are flash-frozen at -179 degrees C diffract to 2.7 A along the c-axis and to 2.4 A in perpendicular directions. The crystals contain one protein-DNA complex in the crystallographic asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Base Sequence
  • Crystallization
  • Crystallography, X-Ray
  • DNA, Fungal / genetics
  • DNA, Fungal / isolation & purification*
  • DNA, Fungal / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / isolation & purification*
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Fungal Proteins / isolation & purification*
  • Homeodomain Proteins*
  • Minor Histocompatibility Antigens
  • Molecular Sequence Data
  • Proto-Oncogene Proteins c-bcl-2*
  • Replication Protein C
  • Repressor Proteins / chemistry
  • Repressor Proteins / genetics
  • Repressor Proteins / isolation & purification*
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins*

Substances

  • BCL2-related protein A1
  • DNA, Fungal
  • DNA-Binding Proteins
  • Fungal Proteins
  • Homeodomain Proteins
  • MATA1 protein, S cerevisiae
  • MATA2 protein, S cerevisiae
  • Minor Histocompatibility Antigens
  • Proto-Oncogene Proteins c-bcl-2
  • Repressor Proteins
  • Saccharomyces cerevisiae Proteins
  • Replication Protein C