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Instruments / Technical Area	Publication Details	Published	Actions
Krios I-Titan Krios I at Diamond	Structural basis for activity switching in polymerases determining the fate of let-7 pre-miRNAs Gangshun Yi , Mingda Ye , Loic Carrique , Afaf H. El-Sagheer , Tom Brown , Chris J. Norbury , Peijun Zhang , Robert J. C. Gilbert Nature Structural & Molecular Biology 20 DOI: 10.1038/s41594-024-01357-9 Diamond Proposal Number(s): [20223, 21004] Open Access Show Abstract ▼ Abstract: Tumor-suppressor let-7 pre-microRNAs (miRNAs) are regulated by terminal uridylyltransferases TUT7 and TUT4 that either promote let-7 maturation by adding a single uridine nucleotide to the pre-miRNA 3′ end or mark them for degradation by the addition of multiple uridines. Oligo-uridylation is increased in cells by enhanced TUT7/4 expression and especially by the RNA-binding pluripotency factor LIN28A. Using cryogenic electron microscopy, we captured high-resolution structures of active forms of TUT7 alone, of TUT7 plus pre-miRNA and of both TUT7 and TUT4 bound with pre-miRNA and LIN28A. Our structures reveal that pre-miRNAs engage the enzymes in fundamentally different ways depending on the presence of LIN28A, which clamps them onto the TUTs to enable processive 3′ oligo-uridylation. This study reveals the molecular basis for mono- versus oligo-uridylation by TUT7/4, as determined by the presence of LIN28A, and thus their mechanism of action in the regulation of cell fate and in cancer.	Jul 2024
	The low-cost Shifter microscope stage transforms the speed and robustness of protein crystal harvesting Nathan David Wright , Patrick Collins , Lizbe Koekemoer , Tobias Krojer , Romain Talon , Elliot Nelson , Mingda Ye , Radoslaw Nowak , Joseph Newman , Jia Tsing Ng , Nick Mitrovic , Helton Wiggers , Frank Von Delft Acta Crystallographica Section D Structural Biology 77, 62 - 74 DOI: 10.1107/S2059798320014114 Open Access Show Abstract ▼ Abstract: Despite the tremendous success of X-ray cryo-crystallography in recent decades, the transfer of crystals from the drops in which they are grown to diffractometer sample mounts remains a manual process in almost all laboratories. Here, the Shifter, a motorized, interactive microscope stage that transforms the entire crystal-mounting workflow from a rate-limiting manual activity to a controllable, high-throughput semi-automated process, is described. By combining the visual acuity and fine motor skills of humans with targeted hardware and software automation, it was possible to transform the speed and robustness of crystal mounting. Control software, triggered by the operator, manoeuvres crystallization plates beneath a clear protective cover, allowing the complete removal of film seals and thereby eliminating the tedium of repetitive seal cutting. The software, either upon request or working from an imported list, controls motors to position crystal drops under a hole in the cover for human mounting at a microscope. The software automatically captures experimental annotations for uploading to the user's data repository, removing the need for manual documentation. The Shifter facilitates mounting rates of 100–240 crystals per hour in a more controlled process than manual mounting, which greatly extends the lifetime of the drops and thus allows a dramatic increase in the number of crystals retrievable from any given drop without loss of X-ray diffraction quality. In 2015, the first in a series of three Shifter devices was deployed as part of the XChem fragment-screening facility at Diamond Light Source, where they have since facilitated the mounting of over 120 000 crystals. The Shifter was engineered to have a simple design, providing a device that could be readily commercialized and widely adopted owing to its low cost. The versatile hardware design allows use beyond fragment screening and protein crystallography.	Jan 2021

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