Crystallization and X-ray diffraction studies of a 434 Cro-DNA complex

J Mol Biol. 1987 Aug 20;196(4):951-4. doi: 10.1016/0022-2836(87)90419-0.

Abstract

Crystals have been obtained of the bacteriophage 434 Cro protein bound to a synthetic DNA operator. An analysis of the packing shows that the complexes stack end-to-end along crystallographic axis, forming long rods with non-crystallographic 11(3) screw symmetry. The average number of DNA base-pairs per turn is 10.27, which is somewhat more overwound as compared with the 434 repressor-DNA crystals of Anderson et al. Diffraction extends to 3 A along the rod direction and to 5 A in perpendicular directions.

Publication types

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

MeSH terms

  • DNA / metabolism*
  • DNA-Binding Proteins*
  • Nucleic Acid Conformation
  • Protein Conformation
  • Repressor Proteins / metabolism*
  • Transcription Factors / metabolism*
  • Viral Proteins
  • Viral Regulatory and Accessory Proteins
  • X-Ray Diffraction

Substances

  • DNA-Binding Proteins
  • Repressor Proteins
  • Transcription Factors
  • Viral Proteins
  • Viral Regulatory and Accessory Proteins
  • phage repressor proteins
  • DNA