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Crystallization of GreA, a transcript cleavage factor from Escherichia coli.

S A Darst·C E Stebbins·S Borukhov·M Orlova·G Feng·R Landick·A Goldfarb
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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.

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Bacterial ProteinsCrystallography, X-RayEscherichia coliTranscription FactorsJournal ArticleResearch Support, Non-U.S. Gov't

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S A Darst, C E Stebbins, S Borukhov, M Orlova, G Feng, R Landick, A Goldfarb. 1994-09-30. Crystallization of GreA, a transcript cleavage factor from Escherichia coli.. https://doi.org/10.1006/jmbi.1994.1603

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