Crystallization of GreA, a transcript cleavage factor from Escherichia coli

Seth A. Darst, Charles E. Stebbins, Sergei Borukhov, Marianna Orlova, Guoha Feng, Robert Landick, Alex 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 propogated by a novel seeding procedure. The crystals diffract beyond 2 AÅ resolution and belong to the orthorhombic space group P212121, with cell dimensions a = 101.7 AÅ, b = 42.22 AÅ, c = 40.05 AÅ and with one molecule in the asymmetric unit.

Original languageEnglish (US)
Pages (from-to)582-585
Number of pages4
JournalJournal of Molecular Biology
Volume242
Issue number4
DOIs
StatePublished - Sep 29 1994

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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    Darst, S. A., Stebbins, C. E., Borukhov, S., Orlova, M., Feng, G., Landick, R., & Goldfarb, A. (1994). Crystallization of GreA, a transcript cleavage factor from Escherichia coli. Journal of Molecular Biology, 242(4), 582-585. https://doi.org/10.1006/jmbi.1994.1603