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Purification, crystallization, and preliminary X‐ray diffraction analysis of even‐skipped homeodomain complexed to DNA
Author(s) -
Hirsch Joel A.,
Aggarwal Aneel K.
Publication year - 1995
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/prot.340210311
Subject(s) - homeobox , crystallography , oligonucleotide , crystallization , sequence (biology) , dna , diffraction , dna sequencing , x ray crystallography , sequence analysis , chemistry , biology , gene , genetics , transcription factor , physics , organic chemistry , optics
Embryonic development in metazoa, to a significant extent, is directed by genes which contain a conserved sequence motif named the homeobox. This sequence encodes a polypeptide called the homeodomain which has sequence specific DNA‐binding activity. We report the purification, crystallization, and preliminary diffraction analysis of the Drosophila Even‐skipped homeodomain (Eve HD) bound to two different oligonucleotides. Crystals of Eve HD complexed with an AT‐rich sequence belong to space group P 2 1 , a = 34.06, b = 61.61, c = 39.99 Å, b=90.0°. These crystals diffract to at least 2.0 Å and both native and derivative data sets have been collected. Crystals of Eve HD complexed with a GC‐rich sequence belong to space group P 6 3 , a = b = 124.52, c = 66.78 Å and diffract to 3.5 Å resolution. A native data set has been collected. © 1995 Wiley‐Liss, Inc.