Crystallization and preliminary X-ray analysis of the β-galactosidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus

Pearl, Laurence H., Hemmings, Andrew M., Nucci, Roberto and Rossi, Mosé (1993) Crystallization and preliminary X-ray analysis of the β-galactosidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus. Journal of Molecular Biology, 229 (2). pp. 561-563. ISSN 0022-2836

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Abstract

The β-galactosidase from the extreme thermophilic archaebacterium sulfolobus solfataricus has been crystallized from polyethylene glycol 4000 in the presence of sodium acetate and acetate buffer at pH 4.6. The protein crystallizes in P3121 or P3221 (a = 169.4, c = 98.29) and the crystals diffract beyond 2.5 AÅ. The measured crystal density (~1.28 g/cm3) is consistent with the presence of a tetramer (molecular mass 240 kDa) in the asymmetric unit. The specific volume of the crystals is 1.7 AÅ3/Da, indicating a solvent content by volume of only 27%, which is amongst the lowest values observed for protein crystals, and indicates virtual close-packing of the tetramers.

Item Type:	Article
Uncontrolled Keywords:	archaebacteria,extreme thermophile,protein thermostability,sulfolobus solfataricus,β-galactosidase,structural biology,molecular biology ,/dk/atira/pure/subjectarea/asjc/1300/1315
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	13 Feb 2025 15:30
Last Modified:	16 Feb 2025 06:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/98468
DOI:	10.1006/jmbi.1993.1057

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