Crystallization and preliminary X-ray analysis of the beta-galactosidase from the extreme thermophilic archaebacterium Sulfolobus solfataricus.
The beta-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 P3(1)21 or P3(2)21 (a = 169.4, c = 98.29) and the crystals diffract beyond 2.5 A. The measured crystal density (approximately 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 A3/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.
Pearl
L H
LH
Department of Biochemistry and Molecular Biology, University College London, U.K.
Hemmings
A M
AM
Nucci
R
R
Rossi
M
M
D003460:Crystallization; D016944:Sulfolobus / Q000201:enzymology*; D014961:X-Ray Diffraction; D001616:beta-Galactosidase / Q000737:chemistry*
D001616:beta-Galactosidase