Crystallographic characterization of Pap1–DNA complex
Acta Crystallographica Section D
Volume 54, Issue 5, pages 1014–1016, September 1998
How to Cite
Fujii, Y., Ohira, T., Kyougoku, Y., Toda, T., Yanagida, M. and Hakoshima, T. (1998), Crystallographic characterization of Pap1–DNA complex. Acta Crystallographica Section D, 54: 1014–1016. doi: 10.1107/S0907444998003266
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Pap1 is a fission yeast transcription factor that activates genes related with resistance against staurosporine, a potent inhibitor of protein kinase C, and has been shown to be involved in cell growth, cell cycle, carcinogenesis and differentiation. Pap1 has the bZIP DNA-binding domain but binds to non-consensus DNA sequences for the bZIP motif. Highly ordered crystals of the DNA-binding domain complexed with a DNA fragment that has an ATF/CREB-like non-consensus sequence have been obtained. The crystals grew by the vapor-diffusion technique with polyethylene glycol 6000 and belong to space group R3 with a = b = 240.78, c = 43.85 Å. A 2.0 Å resolution data set was collected with a cryo-crystallographic technique.