Purification, crystallization and data collection of methicillin-resistant Staphylococcus aureus Sar2676, a pantothenate synthetase

Jaldappagari Seetharamappa; Muse Oke; Huanting Liu; Stephen A McMahon; Kenneth A Johnson; Lester Carter; Mark Dorward; Michal Zawadzki; Ian M Overton; C A Johannes van Niekirk; Shirley Graham; Catherine H Botting; Garry L Taylor; Malcolm F White; Geoffrey J Barton; Peter J Coote; James H Naismith

doi:10.1107/S1744309107020362

Purification, crystallization and data collection of methicillin-resistant Staphylococcus aureus Sar2676, a pantothenate synthetase

Jaldappagari Seetharamappa, Muse Oke, Huanting Liu, Stephen A McMahon, Kenneth A Johnson, Lester Carter, Mark Dorward, Michal Zawadzki, Ian M Overton, C A Johannes van Niekirk, Shirley Graham, Catherine H Botting, Garry L Taylor, Malcolm F White, Geoffrey J Barton, Peter J Coote, James H Naismith

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

Abstract

Sar2676, a pantothenate synthetase with a molecular weight of 31 419 Da from methicillin-resistant Staphylococcus aureus, has been expressed, purified and crystallized at 293 K. The protein crystallizes in a primitive triclinic lattice, with unit-cell parameters a = 45.3, b = 60.5, c = 117.6 A, alpha = 87.2, beta = 81.2, gamma = 68.4 degrees . A complete data set has been collected to 2.3 A resolution at the ESRF. Consideration of the likely solvent content suggested the asymmetric unit to contain four molecules. This has been confirmed by molecular-replacement phasing calculations, which give a solution with four monomers using a monomer of pantothenate synthetase from Escherichia coli (PDB code 1iho), which is 41% identical to Sar2676, as a search model.

Original language	English
Pages (from-to)	488-91
Number of pages	4
Journal	Acta Crystallographica Section F Structural Biology and Crystallization Communications
Volume	63
Issue number	Pt 6
DOIs	https://doi.org/10.1107/S1744309107020362
Publication status	Published - 1 Jun 2007

Keywords

Bacterial Proteins
Crystallization
Crystallography, X-Ray
Methicillin Resistance
Peptide Synthases
Staphylococcus aureus

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Seetharamappa, J., Oke, M., Liu, H., McMahon, S. A., Johnson, K. A., Carter, L., Dorward, M., Zawadzki, M., Overton, I. M., van Niekirk, C. A. J., Graham, S., Botting, C. H., Taylor, G. L., White, M. F., Barton, G. J., Coote, P. J., & Naismith, J. H. (2007). Purification, crystallization and data collection of methicillin-resistant Staphylococcus aureus Sar2676, a pantothenate synthetase. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 63(Pt 6), 488-91. https://doi.org/10.1107/S1744309107020362

Seetharamappa, Jaldappagari ; Oke, Muse ; Liu, Huanting ; McMahon, Stephen A ; Johnson, Kenneth A ; Carter, Lester ; Dorward, Mark ; Zawadzki, Michal ; Overton, Ian M ; van Niekirk, C A Johannes ; Graham, Shirley ; Botting, Catherine H ; Taylor, Garry L ; White, Malcolm F ; Barton, Geoffrey J ; Coote, Peter J ; Naismith, James H. / Purification, crystallization and data collection of methicillin-resistant Staphylococcus aureus Sar2676, a pantothenate synthetase. In: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 2007 ; Vol. 63, No. Pt 6. pp. 488-91.

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title = "Purification, crystallization and data collection of methicillin-resistant Staphylococcus aureus Sar2676, a pantothenate synthetase",

abstract = "Sar2676, a pantothenate synthetase with a molecular weight of 31 419 Da from methicillin-resistant Staphylococcus aureus, has been expressed, purified and crystallized at 293 K. The protein crystallizes in a primitive triclinic lattice, with unit-cell parameters a = 45.3, b = 60.5, c = 117.6 A, alpha = 87.2, beta = 81.2, gamma = 68.4 degrees . A complete data set has been collected to 2.3 A resolution at the ESRF. Consideration of the likely solvent content suggested the asymmetric unit to contain four molecules. This has been confirmed by molecular-replacement phasing calculations, which give a solution with four monomers using a monomer of pantothenate synthetase from Escherichia coli (PDB code 1iho), which is 41% identical to Sar2676, as a search model.",

keywords = "Bacterial Proteins, Crystallization, Crystallography, X-Ray, Methicillin Resistance, Peptide Synthases, Staphylococcus aureus",

author = "Jaldappagari Seetharamappa and Muse Oke and Huanting Liu and McMahon, {Stephen A} and Johnson, {Kenneth A} and Lester Carter and Mark Dorward and Michal Zawadzki and Overton, {Ian M} and {van Niekirk}, {C A Johannes} and Shirley Graham and Botting, {Catherine H} and Taylor, {Garry L} and White, {Malcolm F} and Barton, {Geoffrey J} and Coote, {Peter J} and Naismith, {James H}",

year = "2007",

month = jun,

day = "1",

doi = "10.1107/S1744309107020362",

language = "English",

volume = "63",

pages = "488--91",

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

issn = "1744-3091",

publisher = "Wiley-Blackwell",

number = "Pt 6",

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Seetharamappa, J, Oke, M, Liu, H, McMahon, SA, Johnson, KA, Carter, L, Dorward, M, Zawadzki, M, Overton, IM, van Niekirk, CAJ, Graham, S, Botting, CH, Taylor, GL, White, MF, Barton, GJ, Coote, PJ & Naismith, JH 2007, 'Purification, crystallization and data collection of methicillin-resistant Staphylococcus aureus Sar2676, a pantothenate synthetase', Acta Crystallographica Section F Structural Biology and Crystallization Communications, vol. 63, no. Pt 6, pp. 488-91. https://doi.org/10.1107/S1744309107020362

Purification, crystallization and data collection of methicillin-resistant Staphylococcus aureus Sar2676, a pantothenate synthetase. / Seetharamappa, Jaldappagari; Oke, Muse; Liu, Huanting; McMahon, Stephen A; Johnson, Kenneth A; Carter, Lester; Dorward, Mark; Zawadzki, Michal; Overton, Ian M; van Niekirk, C A Johannes; Graham, Shirley; Botting, Catherine H; Taylor, Garry L; White, Malcolm F; Barton, Geoffrey J; Coote, Peter J; Naismith, James H.

In: Acta Crystallographica Section F Structural Biology and Crystallization Communications, Vol. 63, No. Pt 6, 01.06.2007, p. 488-91.

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

TY - JOUR

T1 - Purification, crystallization and data collection of methicillin-resistant Staphylococcus aureus Sar2676, a pantothenate synthetase

AU - Seetharamappa, Jaldappagari

AU - Oke, Muse

AU - Liu, Huanting

AU - McMahon, Stephen A

AU - Johnson, Kenneth A

AU - Carter, Lester

AU - Dorward, Mark

AU - Zawadzki, Michal

AU - Overton, Ian M

AU - van Niekirk, C A Johannes

AU - Graham, Shirley

AU - Botting, Catherine H

AU - Taylor, Garry L

AU - White, Malcolm F

AU - Barton, Geoffrey J

AU - Coote, Peter J

AU - Naismith, James H

PY - 2007/6/1

Y1 - 2007/6/1

N2 - Sar2676, a pantothenate synthetase with a molecular weight of 31 419 Da from methicillin-resistant Staphylococcus aureus, has been expressed, purified and crystallized at 293 K. The protein crystallizes in a primitive triclinic lattice, with unit-cell parameters a = 45.3, b = 60.5, c = 117.6 A, alpha = 87.2, beta = 81.2, gamma = 68.4 degrees . A complete data set has been collected to 2.3 A resolution at the ESRF. Consideration of the likely solvent content suggested the asymmetric unit to contain four molecules. This has been confirmed by molecular-replacement phasing calculations, which give a solution with four monomers using a monomer of pantothenate synthetase from Escherichia coli (PDB code 1iho), which is 41% identical to Sar2676, as a search model.

AB - Sar2676, a pantothenate synthetase with a molecular weight of 31 419 Da from methicillin-resistant Staphylococcus aureus, has been expressed, purified and crystallized at 293 K. The protein crystallizes in a primitive triclinic lattice, with unit-cell parameters a = 45.3, b = 60.5, c = 117.6 A, alpha = 87.2, beta = 81.2, gamma = 68.4 degrees . A complete data set has been collected to 2.3 A resolution at the ESRF. Consideration of the likely solvent content suggested the asymmetric unit to contain four molecules. This has been confirmed by molecular-replacement phasing calculations, which give a solution with four monomers using a monomer of pantothenate synthetase from Escherichia coli (PDB code 1iho), which is 41% identical to Sar2676, as a search model.

KW - Bacterial Proteins

KW - Crystallization

KW - Crystallography, X-Ray

KW - Methicillin Resistance

KW - Peptide Synthases

KW - Staphylococcus aureus

U2 - 10.1107/S1744309107020362

DO - 10.1107/S1744309107020362

M3 - Article

C2 - 17554169

VL - 63

SP - 488

EP - 491

JO - Acta Crystallographica Section F Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F Structural Biology and Crystallization Communications

SN - 1744-3091

IS - Pt 6

ER -