Crystallization and preliminary X-ray crystallographic studies of response regulator for cyanobacterial phytochrome, Rcp1

Acta Crystallogr D Biol Crystallogr. 2000 Nov;56(Pt 11):1446-8. doi: 10.1107/s0907444900009951.

Abstract

The key response-regulator gene of light regulation, rcp1, from Synechocystis sp. has been overexpressed, purified and subsequently crystallized using ammonium sulfate as a precipitant in forms suitable for X-ray crystallographic studies. A native data set was collected to a resolution of 2.5 A at cryogenic temperature. The crystals belong to the hexagonal space group P6(3), with unit-cell parameters a = b = 89.04 (5), c = 60.29 (3) A. The Matthews parameter suggests that Rcp1 crystallizes with two molecules per asymmetric unit.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins*
  • Crystallization
  • Crystallography, X-Ray
  • Cyanobacteria / chemistry*
  • Molecular Sequence Data
  • Proteins / chemistry*
  • Sequence Homology, Amino Acid

Substances

  • Bacterial Proteins
  • Proteins
  • Rcp1 protein, Synechocystis