title: Crystallization of GreA, a transcript cleavage factor from Escherichia coli.
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.
authors.affiliation: Rockefeller University, New York, NY 10021.
authors.forename: S A
authors.initials: SA
authors.lastname: Darst
authors.forename: C E
authors.initials: CE
authors.lastname: Stebbins
authors.forename: S
authors.initials: S
authors.lastname: Borukhov
authors.forename: M
authors.initials: M
authors.lastname: Orlova
authors.forename: G
authors.initials: G
authors.lastname: Feng
authors.forename: R
authors.initials: R
authors.lastname: Landick
authors.forename: A
authors.initials: A
authors.lastname: Goldfarb
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D014157:Transcription Factors
chemical_list: D001426:Bacterial Proteins; D014157:Transcription Factors; C075886:GREA protein, Rickettsia prowazekii