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Expression, purification, and crystallization of the DNA‐binding domain from the Saccharomyces cerevisae cell‐cycle transcription factor MBP‐1
Author(s) -
Taylor Ian A.,
Smerdon Stephen J.
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199702)27:2<325::aid-prot20>3.0.co;2-n
Subject(s) - transcription factor , dna binding domain , microbiology and biotechnology , dna , crystallization , biology , transcription (linguistics) , dna binding protein , domain (mathematical analysis) , cell cycle , computational biology , chemistry , genetics , cell , gene , mathematics , linguistics , philosophy , organic chemistry , mathematical analysis
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 = b = 42.2 Å, c = 123.2 Å and a monomer in the asymmetric unit. © 1997 Wiley‐Liss, Inc.