Abstract
Dysfunction of histone-modifying enzymes affects chromatin regulation and is involved in carcinogenesis, tumour progression and other diseases. Histone methyltransferases are a family of key histone-modifying enzymes, but their structures, functions and mechanisms are incompletely understood, thus constraining drug-design efforts. Here, preliminary steps towards structure-function studies of Schizosaccharomyces pombe Set7, a putative histone methyltransferase and the first yeast full-length SET-domain-containing protein to be studied using X-ray crystallography, are reported. The methods from cloning to X-ray diffraction and phasing are discussed and the results will aid in prospective studies of histone-modifying enzymes.
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Mevius, D. E. H. F., Shen, Y., Morishita, M., & Di Luccio, E. (2016). Cloning, expression, purification and crystallization of Schizosaccharomyces pombe Set7, a putative histone methyltransferase. Acta Crystallographica Section:F Structural Biology Communications, 72, 263–268. https://doi.org/10.1107/S2053230X16003794
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