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 journalArticlepeer-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 languageEnglish
Pages (from-to)228-230
Number of pages3
JournalActa Crystallographica. Section F, Structural biology and crystallization communications
Volume62
DOIs
Publication statusPublished - Mar 2006

Keywords

  • NOV.

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  • BBSRC BBS/B/14426: SPORT

    Naismith, J.

    BBSRC

    18/10/0430/04/12

    Project: Standard

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