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Crystal structure of the Escherichia coli transcription termination factor Rho

Fan, Chengcheng and Rees, Douglas C. (2020) Crystal structure of the Escherichia coli transcription termination factor Rho. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 76 (9). Art. No. F76. ISSN 2053-230X. PMCID PMC7470046. doi:10.1107/s2053230x20010572.

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During the crystal structure analysis of an ATP-binding cassette (ABC) transporter overexpressed in Escherichia coli, a contaminant protein was crystallized. The identity of the contaminant was revealed by mass spectrometry to be the Escherichia coli transcription terminator factor Rho, structures of which had been previously determined in different conformational states. Although Rho was present at only ∼1% of the target protein (a bacterial homolog of the eukaryotic ABC transporter of mitochondria from Novosphingobium aromaticivorans; NaAtm1), it preferentially crystallized in space group C2 as thin plates that diffracted to 3.30 Å resolution. The structure of Rho in this crystal form exhibits a hexameric open-ring staircase conformation with bound ATP; this characteristic structure was also observed on electron-microscopy grids of the NaAtm1 preparation.

Item Type:Article
Related URLs:
URLURL TypeDescription ItemSupporting Information ItemSupporting Information CentralArticle
Fan, Chengcheng0000-0003-4213-5758
Rees, Douglas C.0000-0003-4073-1185
Additional Information:© 2020 International Union of Crystallography. Received 7 April 2020; Accepted 31 July 2020. The following funding is acknowledged: Howard Hughes Medical Institute.
Funding AgencyGrant Number
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Subject Keywords:membrane-protein purification; crystallization contaminant; transcription termination factor; cryoEM
Issue or Number:9
PubMed Central ID:PMC7470046
Record Number:CaltechAUTHORS:20200828-111354696
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Official Citation:Crystal structure of the Escherichia coli transcription termination factor Rho. Fan, C. & Rees, D. C. (2020). Acta Cryst. F76; doi: 10.1107/s2053230x20010572
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:105139
Deposited By: Tony Diaz
Deposited On:28 Aug 2020 21:21
Last Modified:16 Nov 2021 18:40

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