From SubPAR to PAR, into the CryoEM, and More Macrolides

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From SubPAR to PAR, into the CryoEM, and More Macrolides   Cell Chemical Biology  Volume 23, Issue 6, Pages 635-636 (June 2016) DOI: 10.1016/j.chembiol.2016.06.004 Copyright © 2016 Terms and Conditions

Gibson et al. use an analog-sensitive strategy to control the poly(ADP-ribosyl) transferase reaction in cells. Chains of ADP-ribosyls are efficiently formed and amenable to different types of analysis and manipulation. (Image by Toni Lozano, via Wikimedia Commons.) Cell Chemical Biology 2016 23, 635-636DOI: (10.1016/j.chembiol.2016.06.004) Copyright © 2016 Terms and Conditions

Resolution of structures solved by cryo-electron microscopy (cryoEM) has been steadily improving. Merk et al., and all of us, find ourselves at the beginning of a new chapter in the cryoEM era in which images of even smaller proteins and the small molecules they bind, are sharp and crisp, inviting us to take a closer look and then stay awhile. Cell Chemical Biology 2016 23, 635-636DOI: (10.1016/j.chembiol.2016.06.004) Copyright © 2016 Terms and Conditions

Erythromycin and other macrolide antibiotics, in general, have complex chemical structures, and they have not been easy to synthesize de novo and derivatize through semi-synthetic strategies. Seiple et al. now present a remarkable way to make a variety of macrolide antibiotics and make them readily available for antibacterial activity validation. Cell Chemical Biology 2016 23, 635-636DOI: (10.1016/j.chembiol.2016.06.004) Copyright © 2016 Terms and Conditions