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

Laurence H. Pearl; Andrew M. Hemmings; Roberto Nucci; Mosé Rossi

doi:10.1006/jmbi.1993.1057

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

Laurence H. Pearl, Andrew M. Hemmings, Roberto Nucci, Mosé Rossi

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

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.

Original language	English
Pages (from-to)	561-563
Number of pages	3
Journal	Journal of Molecular Biology
Volume	229
Issue number	2
DOIs	https://doi.org/10.1006/jmbi.1993.1057
Publication status	Published - 20 Jan 1993
Externally published	Yes

Keywords

archaebacteria
extreme thermophile
Protein thermostability
Sulfolobus solfataricus
β-galactosidase

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10.1006/jmbi.1993.1057

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

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 A{\AA}. 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 A{\AA}3/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.",

keywords = "archaebacteria, extreme thermophile, Protein thermostability, Sulfolobus solfataricus, β-galactosidase",

author = "Pearl, {Laurence H.} and Hemmings, {Andrew M.} and Roberto Nucci and Mos{\'e} Rossi",

year = "1993",

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T1 - Crystallization and preliminary X-ray analysis of the β-galactosidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus

AU - Pearl, Laurence H.

AU - Hemmings, Andrew M.

AU - Nucci, Roberto

AU - Rossi, Mosé

PY - 1993/1/20

Y1 - 1993/1/20

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AB - 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.

KW - archaebacteria

KW - extreme thermophile

KW - Protein thermostability

KW - Sulfolobus solfataricus

KW - β-galactosidase

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

Abstract

Keywords

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