Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the C-terminal domain of Ss-LrpB, a transcription regulator from Sulfolobus solfataricus.
Ss-LrpB from Sulfolobus solfataricus P2 belongs to the bacterial/archaeal superfamily of Lrp-like (leucine-responsive regulatory protein-like) transcription regulators. The N-terminal DNA-binding domain contains a HTH motif and the C-terminal domain contains an alphabeta-sandwich (betaalphabetabetaalphabeta fold). The C-terminal domain was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 59.35, b = 74.86, c = 38.08 A and a data set was collected to 2.0 A resolution. Structure determination using a selenomethionine derivative is under way.
Peeters
Eveline
E
Erfelijkheidsleer en Microbiologie, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels, Belgium.
Hoa
Bach Thi Mai
BT
Zegers
Ingrid
I
Charlier
Daniel
D
Maes
Dominique
D
D020816:Amino Acid Motifs; D019843:Archaeal Proteins / Q000737:chemistry*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D007930:Leucine / Q000737:chemistry; D016133:Polymerase Chain Reaction; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D048229:Sulfolobus solfataricus / Q000378:metabolism*; D013696:Temperature; D014157:Transcription Factors / Q000737:chemistry*; D014158:Transcription, Genetic; D014961:X-Ray Diffraction / Q000379:methods*
D019843:Archaeal Proteins; D014157:Transcription Factors; D007930:Leucine