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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 | |
| Publication status | Published - Mar 2006 |
Keywords
- NOV.
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- 1 Finished
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BBSRC BBS/B/14426: SPORT
Naismith, J. (PI)
Biotechnology and Biological Sciences Research Council
18/10/04 → 30/04/12
Project: Standard
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