Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide

Julie Wolfová; Jeroen R. Mesters; Jiří Brynda; Rita Grandori; Antonino Natalello; Jannette Carey; Ivana Kutá Smatanová

doi:10.1107/S1744309107026103

Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide

Julie Wolfová, Jeroen R. Mesters, Jiří Brynda, Rita Grandori, Antonino Natalello, Jannette Carey, Ivana Kutá Smatanová^*

^*Corresponding author for this work

Institute of Biochemistry

5 Citations (Scopus)

Abstract

The flavoprotein WrbA from Escherichia coli is considered to be the prototype of a new family of multimeric flavodoxin-like proteins that are implicated in cell protection against oxidative stress. The present study is aimed at structural characterization of the E. coli protein with respect to its recently revealed oxidoreductase activity. Crystals of WrbA holoprotein in complex with the oxidized flavin cofactor (FMN) were obtained using standard vapour-diffusion techniques. Deep yellow tetragonal crystals obtained from differing crystallization conditions display different space groups and unit-cell parameters. X-ray crystal structures of the WrbA holoprotein have been determined to resolutions of 2.0 and 2.6 Å.

Original language	English
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	63
Issue number	7
Pages (from-to)	571-575
Number of pages	5
ISSN	1744-3091
DOIs	https://doi.org/10.1107/S1744309107026103
Publication status	Published - 15.06.2007

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Research Areas and Centers

Academic Focus: Center for Infection and Inflammation Research (ZIEL)

Access to Document

10.1107/S1744309107026103

Cite this

Wolfová, J., Mesters, J. R., Brynda, J., Grandori, R., Natalello, A., Carey, J., & Kutá Smatanová, I. (2007). Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 63(7), 571-575. https://doi.org/10.1107/S1744309107026103

@article{04ff4292fe4e4397a917e4d60ac9f1d4,

title = "Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide",

abstract = "The flavoprotein WrbA from Escherichia coli is considered to be the prototype of a new family of multimeric flavodoxin-like proteins that are implicated in cell protection against oxidative stress. The present study is aimed at structural characterization of the E. coli protein with respect to its recently revealed oxidoreductase activity. Crystals of WrbA holoprotein in complex with the oxidized flavin cofactor (FMN) were obtained using standard vapour-diffusion techniques. Deep yellow tetragonal crystals obtained from differing crystallization conditions display different space groups and unit-cell parameters. X-ray crystal structures of the WrbA holoprotein have been determined to resolutions of 2.0 and 2.6 {\AA}.",

author = "Julie Wolfov{\'a} and Mesters, \{Jeroen R.\} and Ji{\v r}{\'i} Brynda and Rita Grandori and Antonino Natalello and Jannette Carey and \{Kut{\'a} Smatanov{\'a}\}, Ivana",

year = "2007",

month = jun,

day = "15",

doi = "10.1107/S1744309107026103",

language = "English",

volume = "63",

pages = "571--575",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

issn = "1744-3091",

number = "7",

}

Wolfová, J, Mesters, JR, Brynda, J, Grandori, R, Natalello, A, Carey, J & Kutá Smatanová, I 2007, 'Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 63, no. 7, pp. 571-575. https://doi.org/10.1107/S1744309107026103

Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide. / Wolfová, Julie; Mesters, Jeroen R.; Brynda, Jiří et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 63, No. 7, 15.06.2007, p. 571-575.

Research output: Journal Articles › Journal articles › Research › peer-review

TY - JOUR

T1 - Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide

AU - Wolfová, Julie

AU - Mesters, Jeroen R.

AU - Brynda, Jiří

AU - Grandori, Rita

AU - Natalello, Antonino

AU - Carey, Jannette

AU - Kutá Smatanová, Ivana

PY - 2007/6/15

Y1 - 2007/6/15

N2 - The flavoprotein WrbA from Escherichia coli is considered to be the prototype of a new family of multimeric flavodoxin-like proteins that are implicated in cell protection against oxidative stress. The present study is aimed at structural characterization of the E. coli protein with respect to its recently revealed oxidoreductase activity. Crystals of WrbA holoprotein in complex with the oxidized flavin cofactor (FMN) were obtained using standard vapour-diffusion techniques. Deep yellow tetragonal crystals obtained from differing crystallization conditions display different space groups and unit-cell parameters. X-ray crystal structures of the WrbA holoprotein have been determined to resolutions of 2.0 and 2.6 Å.

AB - The flavoprotein WrbA from Escherichia coli is considered to be the prototype of a new family of multimeric flavodoxin-like proteins that are implicated in cell protection against oxidative stress. The present study is aimed at structural characterization of the E. coli protein with respect to its recently revealed oxidoreductase activity. Crystals of WrbA holoprotein in complex with the oxidized flavin cofactor (FMN) were obtained using standard vapour-diffusion techniques. Deep yellow tetragonal crystals obtained from differing crystallization conditions display different space groups and unit-cell parameters. X-ray crystal structures of the WrbA holoprotein have been determined to resolutions of 2.0 and 2.6 Å.

UR - https://www.scopus.com/pages/publications/34447327214

U2 - 10.1107/S1744309107026103

DO - 10.1107/S1744309107026103

M3 - Journal articles

C2 - 17620713

AN - SCOPUS:34447327214

SN - 1744-3091

VL - 63

SP - 571

EP - 575

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 7

ER -

Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide

Abstract

UN SDGs

Research Areas and Centers

Access to Document

Other files and links

Fingerprint

Cite this