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

doi:10.1006/jmbi.1994.1603

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

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

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 language	American English
Pages (from-to)	582-585
Number of pages	4
Journal	Journal of molecular biology
Volume	242
Issue number	4
DOIs	https://doi.org/10.1006/jmbi.1994.1603
State	Published - Sep 29 1994
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Structural Biology
Molecular Biology

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10.1006/jmbi.1994.1603

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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 propogated by a novel seeding procedure. The crystals diffract beyond 2 A{\AA} resolution and belong to the orthorhombic space group P212121, with cell dimensions a = 101.7 A{\AA}, b = 42.22 A{\AA}, c = 40.05 A{\AA} and with one molecule in the asymmetric unit.",

author = "Darst, \{Seth A.\} and Stebbins, \{Charles E.\} and Sergei Borukhov and Marianna Orlova and Guoha Feng and Robert Landick and Alex Goldfarb",

year = "1994",

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day = "29",

doi = "10.1006/jmbi.1994.1603",

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volume = "242",

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journal = "Journal of molecular biology",

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T1 - Crystallization of GreA, a transcript cleavage factor from Escherichia coli

AU - Darst, Seth A.

AU - Stebbins, Charles E.

AU - Borukhov, Sergei

AU - Orlova, Marianna

AU - Feng, Guoha

AU - Landick, Robert

AU - Goldfarb, Alex

PY - 1994/9/29

Y1 - 1994/9/29

N2 - 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.

AB - 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.

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DO - 10.1006/jmbi.1994.1603

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SN - 0022-2836

VL - 242

SP - 582

EP - 585

JO - Journal of molecular biology

JF - Journal of molecular biology

IS - 4

ER -

Crystallization of GreA, a transcript cleavage factor from Escherichia coli

Abstract

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