Overexpression, purification, crystallization and data collection of Sulfolobus solfataricus Sso6206, a novel highly conserved protein

A R McEwan; H Liu; M Oke; L Carter; H Powers; M Dorward; SA MacMahon; Malcolm Frederick White; James Henderson Naismith

doi:10.1107/S1744309106003654

Overexpression, purification, crystallization and data collection of Sulfolobus solfataricus Sso6206, a novel highly conserved protein

A R McEwan, H Liu, M Oke, L Carter, H Powers, M Dorward, SA MacMahon, Malcolm Frederick White, James Henderson Naismith

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

Abstract

Sso6206, a 10.5 kDa protein from Sulfolobus solfataricus, has been over-expressed, purified and crystallized. The protein crystallizes in space group P6(1/5)22, with unit-cell parameters a = b = 157.8, c = 307.3 angstrom. The crystals are hexagonal bipyramids and a data set has been collected to 2.4 angstrom resolution. Molecular replacement cannot be attempted as no convincing model can be identified. Crystals of selenomethionine-variant protein have not yet been obtained. Interestingly, crystal packing, gel filtration and mass spectrometry all suggest the native protein forms a multi-subunit oligomer consisting of > 9 subunits.

Original language	English
Pages (from-to)	228-230
Number of pages	3
Journal	Acta Crystallographica. Section F, Structural biology and crystallization communications
Volume	62
DOIs	https://doi.org/10.1107/S1744309106003654
Publication status	Published - Mar 2006

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NOV.

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10.1107/S1744309106003654

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McEwan, A. R., Liu, H., Oke, M., Carter, L., Powers, H., Dorward, M., MacMahon, SA., White, M. F., & Naismith, J. H. (2006). Overexpression, purification, crystallization and data collection of Sulfolobus solfataricus Sso6206, a novel highly conserved protein. Acta Crystallographica. Section F, Structural biology and crystallization communications , 62, 228-230. https://doi.org/10.1107/S1744309106003654

@article{ee2972066f3844fdb96b42d220321746,

title = "Overexpression, purification, crystallization and data collection of Sulfolobus solfataricus Sso6206, a novel highly conserved protein",

abstract = "Sso6206, a 10.5 kDa protein from Sulfolobus solfataricus, has been over-expressed, purified and crystallized. The protein crystallizes in space group P6(1/5)22, with unit-cell parameters a = b = 157.8, c = 307.3 angstrom. The crystals are hexagonal bipyramids and a data set has been collected to 2.4 angstrom resolution. Molecular replacement cannot be attempted as no convincing model can be identified. Crystals of selenomethionine-variant protein have not yet been obtained. Interestingly, crystal packing, gel filtration and mass spectrometry all suggest the native protein forms a multi-subunit oligomer consisting of > 9 subunits.",

keywords = "NOV.",

author = "McEwan, {A R} and H Liu and M Oke and L Carter and H Powers and M Dorward and SA MacMahon and White, {Malcolm Frederick} and Naismith, {James Henderson}",

year = "2006",

month = mar,

doi = "10.1107/S1744309106003654",

language = "English",

volume = "62",

pages = "228--230",

journal = "Acta Crystallographica. Section F, Structural biology and crystallization communications ",

issn = "1744-3091",

publisher = "Wiley-Blackwell",

}

McEwan, AR, Liu, H, Oke, M, Carter, L, Powers, H, Dorward, M, MacMahon, SA, White, MF & Naismith, JH 2006, 'Overexpression, purification, crystallization and data collection of Sulfolobus solfataricus Sso6206, a novel highly conserved protein', Acta Crystallographica. Section F, Structural biology and crystallization communications , vol. 62, pp. 228-230. https://doi.org/10.1107/S1744309106003654

TY - JOUR

T1 - Overexpression, purification, crystallization and data collection of Sulfolobus solfataricus Sso6206, a novel highly conserved protein

AU - McEwan, A R

AU - Liu, H

AU - Oke, M

AU - Carter, L

AU - Powers, H

AU - Dorward, M

AU - MacMahon, SA

AU - White, Malcolm Frederick

AU - Naismith, James Henderson

PY - 2006/3

Y1 - 2006/3

N2 - Sso6206, a 10.5 kDa protein from Sulfolobus solfataricus, has been over-expressed, purified and crystallized. The protein crystallizes in space group P6(1/5)22, with unit-cell parameters a = b = 157.8, c = 307.3 angstrom. The crystals are hexagonal bipyramids and a data set has been collected to 2.4 angstrom resolution. Molecular replacement cannot be attempted as no convincing model can be identified. Crystals of selenomethionine-variant protein have not yet been obtained. Interestingly, crystal packing, gel filtration and mass spectrometry all suggest the native protein forms a multi-subunit oligomer consisting of > 9 subunits.

AB - Sso6206, a 10.5 kDa protein from Sulfolobus solfataricus, has been over-expressed, purified and crystallized. The protein crystallizes in space group P6(1/5)22, with unit-cell parameters a = b = 157.8, c = 307.3 angstrom. The crystals are hexagonal bipyramids and a data set has been collected to 2.4 angstrom resolution. Molecular replacement cannot be attempted as no convincing model can be identified. Crystals of selenomethionine-variant protein have not yet been obtained. Interestingly, crystal packing, gel filtration and mass spectrometry all suggest the native protein forms a multi-subunit oligomer consisting of > 9 subunits.

KW - NOV.

UR - http://www.scopus.com/inward/record.url?scp=33645749414&partnerID=8YFLogxK

UR - http://ukpmc.ac.uk/abstract/MED/16511308

U2 - 10.1107/S1744309106003654

DO - 10.1107/S1744309106003654

M3 - Article

SN - 1744-3091

VL - 62

SP - 228

EP - 230

JO - Acta Crystallographica. Section F, Structural biology and crystallization communications

JF - Acta Crystallographica. Section F, Structural biology and crystallization communications

ER -

Overexpression, purification, crystallization and data collection of Sulfolobus solfataricus Sso6206, a novel highly conserved protein

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BBSRC BBS/B/14426: SPORT

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Overexpression, purification, crystallization and data collection of Sulfolobus solfataricus Sso6206, a novel highly conserved protein

Abstract

Keywords

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BBSRC BBS/B/14426: SPORT

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