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