Expression, purification, and crystallization of the DNA-binding domain from the Saccharomyces cerevisae cell-cycle transcription factor MBP-1

✍ Scribed by Ian A. Taylor; Stephen J. Smerdon

• Publisher: John Wiley and Sons
• Year: 1997
• Tongue: English
• Weight: 31 KB
• Volume: 27
• Category: Article
• ISSN: 0887-3585
• DOI: 10.1002/(sici)1097-0134(199702)27:2<325::aid-prot20>3.0.co;2-n

✦ Synopsis

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 Å resolution. The space group is tetragonal, P4 3 2 1 2 or P4 1 2 1 2 with unit cell dimensions a 5 b 5 42.2 Å, c 5 123.2 Å and a monomer in the asymmetric unit. Proteins 27:325-327 r 1997 Wiley-Liss, Inc.