News

In Tallahassee, Florida, I had the privilege to participate in the 90th birthday celebration for Don Caspar, as I will report in another note. Andrew Brown, the last speaker of that Symposium organized at Florida State University gave a historical account of J D Bernal, a physicist who crossed paths with Don early on and must have been quite influential for his thinking. Now what interested me greatly is that Bernal, as early as 1931, well before the discovery...

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The new Krios Titan of Columbia University has just been installed at NYSBC. We expect it to be fully operational as part of the Columbia cryo-EM facility in February, ahead of schedule.


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Advances in the field of single-particle cryo-electron microscopy over the last decade. Joachim Frank. In single-particle cryo-electron microscopy (cryo-EM), molecules suspended in a thin aqueous layer are rapidly frozen and imaged at cryogenic temperature in the transmission electron microscope. From the random projection views, a three dimensional image is reconstructed, enabling the structure of the molecule to be obtained. In this article I discuss technological progress over the past decade, which has, in my own field of study, culminated in the determination of ribosome structure...

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Following termination of protein synthesis, bacterial ribosomes are split into subunits by the joint action of elongation factor G and ribosome recycling factor in the process called ribosome recycling. In this issue of Structure, Fu et al. (2016) describe visualization of transient intermediates of ribosome recycling using time-resolved cryogenic electron microscopy. Read more by clicking here.

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I was very sad to hear that Klaus Schulten passed away on November 1 after several months of illness. He was an enthusiastic collaborator and friend for more than a decade. We had just submitted a joint paper on a general method of describing domain motions in molecular machines for the Festschrift planned for the celebration of his 70^th birthday. Our earlier collaborations, in which his students Elizabeth Villa and Leonardo Trabuco played...

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Our paper describing the 2.5-Å structure of the large ribosomal subunit of T. cruzi has finally appeared. It presents a culmination of a collaboration of four groups: our own lab, Susan Madison Antennucci’s at the Wadsworth Center in Albany, Liang Tong’s at the Department of Biological Sciences, also Columbia University, and John Woolford’s at Carnegie Mellon University in Pittsburgh. “Structure and assembly...

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Our long-awaited Cell article on the activation and gating mechanism of the skeletal Ryanodine receptor RyR1 (a.k.a. calcium release channel) has finally appeared in Cell [1]. It is based on the highest-resolution maps obtained so far (up to 3.6 Å), which depict the channel in several states induced by the binding of calcium, ATP and caffeine, including a fully open state. The atomic structures determined from these density maps allowed us to infer the mechanisms of channel activation and gating, as sketched out in the graphical abstract below. Our article follows an earlier paper by Nieng Yan’s...

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Congratulations to Dr. Ming Sun for her successful thesis defense on Thursday, July 14, 2016. The title of her Ph.D. thesis is “Cryo-Electron Microscopy Studies of Dynamical Features of Ribosomes During the Translation Process.” Members of her Thesis Committee: Ruben Gonzalez (Chair), Joachim Frank (Sponsor/Mentor), Wayne Hendrickson, Bridget Carragher, and Jeffrey Dvorin (Children’s Hospital, Harvard Medical School)

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Structural basis for gating and activation of RyR1. by Amédée des Georges, Oliver B. Clarke, Ran Zalk, Qi Yuan, Kendall J. Condon, Robert A. Grassucci, Wayne A. Hendrickson, Andrew R. Marks, and Joachim Frank. Several reconstructions, in the range of 3.6 to 4.4A resolution, portray the structures in open and closed states of the channel and provide clues on the mechanisms of activation and gating, which are mediated by long-range allosteric coupling. In contrast, the papers published in Nature last year by us and two other groups show the channel in the closed state.

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Elucidation of AMPA receptor–stargazin complexes by cryo–electron microscopy. by Edward C. Twomey, Maria V. Yelshanskaya, Robert A. Grassucci, Joachim Frank, and
Alexander I. Sobolevsky. Abstract: AMPA-subtype ionotropic glutamate receptors (AMPARs) mediate fast excitatory neurotransmission and contribute to high cognitive processes such as learning and memory. In the brain, AMPAR trafficking, gating, and pharmacology is tightly controlled by transmembrane AMPAR regulatory proteins...

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