Cloning, expression, crystallization and preliminary X-ray analysis of the DNA-binding protein Sso10a from Sulfolobus solfataricus.
The gene for the DNA-binding protein Sso10a from the hyperthermophilic archaeon Sulfolobus solfataricus was cloned and overexpressed in Escherichia coli. Crystals of the purified protein have been grown that diffract to beyond 2.15 A resolution. The protein crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 57.24, b = 60.16, c = 69.96 A. With one dimer per asymmetric unit, the crystal to volume per protein mass (V(M)) is 2.9 A(3) Da(-1) and the solvent content is approximately 57%. Complete X-ray diffraction native data were collected from a single crystal and processed to 2.15 A.
Teale
M J
MJ
Chemistry Department, University of Alabama in Huntsville, Huntsville, AL 35899, USA. tealem@email.uah.edu
Kahsai
M
M
Singh
S K
SK
Edmondson
S P
SP
Gupta
R
R
Shriver
J W
JW
Meehan
E
E
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D016415:Sequence Alignment; D016944:Sulfolobus / Q000737:chemistry*; D014961:X-Ray Diffraction
D019843:Archaeal Proteins; D004268:DNA-Binding Proteins