Purification, crystallization, and preliminary X-ray diffraction analysis of even-skipped homeodomain complexed to DNA.
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 P2(1), a = 34.06, b = 61.61, c = 39.99 Angstrom, beta = 90.0 degrees. These crystals diffract to at least 2.0 Angstrom and both native and derivative data sets have been collected. Crystals of Eve HD complexed with a GC-rich sequence belong to space group P6(3), a = b = 124.52, c = 66.78 Angstrom and diffract to 3.5 Angstrom resolution. A native data set has been collected.[1]References
- Purification, crystallization, and preliminary X-ray diffraction analysis of even-skipped homeodomain complexed to DNA. Hirsch, J.A., Aggarwal, A.K. Proteins (1995) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
