Crystallization of GreA, a transcript cleavage factor from Escherichia coli

J Mol Biol. 1994 Sep 30;242(4):582-5. doi: 10.1006/jmbi.1994.1603.

Abstract

GreA is a 17.6 kDa protein from Escherichia coli that induces cleavage of the nascent transcript in the elongating complex of RNA polymerase, followed by release of the 3'-terminal fragment. Crystals of GreA have been obtained from polyethylene glycol 4000, 2-propanol and sodium citrate, pH 5.6 and have been propagated by a novel seeding procedure. The crystals diffract beyond 2 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with cell dimensions a = 101.7 A, b = 42.22 A, c = 40.05 A and with one molecule in the asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Crystallography, X-Ray
  • Escherichia coli*
  • Transcription Factors*

Substances

  • Bacterial Proteins
  • Transcription Factors
  • GREA protein, Rickettsia prowazekii