Expression, purification, and crystallization of the DNA-binding domain from the Saccharomyces cerevisae cell-cycle transcription factor MBP-1.
A 124-residue N-terminal fragment corresponding to the DNA-binding domain of the Saccharomyces cerevisae cell-cycle transcription factor MBP-1 has been expressed with a hexahistidine affinity tag in E. coli and purified to apparent homogeneity. Crystals have been grown using PEG 3350 as precipitant which diffract x-rays to greater than 2.6 A resolution. The space group is tetragonal, P4(3)2(1)2 or P4(1)2(1)2 with unit cell dimensions a = b = 42.2 A, c = 123.2 A and a monomer in the asymmetric unit.
Taylor
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Division of Protein Structure, National Institute for Medical Research, London, U.K.
Smerdon
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SJ
D001665:Binding Sites; D002453:Cell Cycle; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D005656:Fungal Proteins; C083209:MBP1 protein, S cerevisiae; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors