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Purification, crystallization and data collection of Pectobacterium chrysanthemi AcsD, a type A siderophore synthetase

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McMahon, Stephen A., Oke, Muse, Liu, Huanting, Johnson, K. A. (Kenneth A.), Carter, Lester, Kadi, Nadia, White, Malcolm F., Challis, Gregory L. and Naismith, James H.. (2008) Purification, crystallization and data collection of Pectobacterium chrysanthemi AcsD, a type A siderophore synthetase. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, Vol.64 (Pt.11). pp. 1052-1055. ISSN 1744-3091

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Official URL: http://dx.doi.org/10.1107/S1744309108032132

Abstract

AcsD, a type A siderophore synthetase with a molecular weight of 71 140 Da from Pectobacterium chrysanthemi, has been expressed, purified and crystallized at 293 K. The protein crystallized in the primitive orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 80.3, b = 95.7, c = 161.1 angstrom, alpha = beta = gamma = 90 degrees. Systematic absences were consistent with space group P2(1)2(1)2(1). A complete data set has been collected to 2.25 angstrom resolution on BM14 at the ESRF. Consideration of the likely solvent content suggested that the asymmetric unit contained two molecules. Gel-filtration experiments indicated that the protein was a dimer, although self-rotation analyses did not detect a convincing twofold symmetry axis in the asymmetric unit. The protein has no convincing sequence match to any known structure and thus solution is likely to require experimental phasing.

Item Type:

Journal Article

Subjects:

Q Science > QD Chemistry
Q Science > QR Microbiology

Divisions:

Faculty of Science > Chemistry

Library of Congress Subject Headings (LCSH):

Siderophores -- Synthesis, Crystallization, Erwinia, Ligases, Iron

Journal or Publication Title:

Acta Crystallographica. Section F: Structural Biology and Crystallization Communications

Publisher:

Wiley-Blackwell Publishing, Inc.

ISSN:

1744-3091

Official Date:

November 2008

Dates:

Date	Event
November 2008	Published

Volume:

Vol.64

Number:

Pt.11

Number of Pages:

Page Range:

pp. 1052-1055

Identification Number:

10.1107/S1744309108032132

Status:

Peer Reviewed

Publication Status:

Published

Access rights to Published version:

Restricted or Subscription Access

Funder:

Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Scottish Higher Education Funding Council (SHEFC)

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