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Instruments / Technical Area	Publication Details	Published	Actions
	Droplet microfluidics for time-resolved serial crystallography Jack Stubbs , Theo Hornsey , Niall Hanrahan , Luis Blay Esteban , Rachel Bolton , Martin Maly , Shibom Basu , Julien Orlans , Daniele De Sanctis , Jung-Uk Shim , Patrick D. Shaw Stewart , Allen M. Orville , Ivo Tews , Jonathan West Iucrj 11, 237 - 248 DOI: 10.1107/S2052252524001799 Open Access Show Abstract ▼ Abstract: Serial crystallography requires large numbers of microcrystals and robust strategies to rapidly apply substrates to initiate reactions in time-resolved studies. Here, we report the use of droplet miniaturization for the controlled production of uniform crystals, providing an avenue for controlled substrate addition and synchronous reaction initiation. The approach was evaluated using two enzymatic systems, yielding 3 µm crystals of lysozyme and 2 µm crystals of Pdx1, an Arabidopsis enzyme involved in vitamin B6 biosynthesis. A seeding strategy was used to overcome the improbability of Pdx1 nucleation occurring with diminishing droplet volumes. Convection within droplets was exploited for rapid crystal mixing with ligands. Mixing times of <2 ms were achieved. Droplet microfluidics for crystal size engineering and rapid micromixing can be utilized to advance time-resolved serial crystallography.	Mar 2024
I24-Microfocus Macromolecular Crystallography	Ternary structure reveals mechanism of a membrane diacylglycerol kinase Dianfan Li , Phillip J. Stansfeld , Mark S. P. Sansom , Aaron Keogh , Lutz Vogeley , Nicole Howe , Joseph Lyons , David Aragao , Petra Fromme , Raimund Fromme , Shibom Basu , Ingo Grotjohann , Christopher Kupitz , Kimberley Rendek , Uwe Weierstall , Nadia A. Zatsepin , Vadim Cherezov , Wei Liu , Sateesh Bandaru , Niall J. English , Cornelius Gati , Anton Barty , Oleksandr Yefanov , Henry N. Chapman , Kay Diederichs , Marc Messerschmidt , Sébastien Boutet , Garth J. Williams , M. Marvin Seibert , Martin Caffrey Nature Communications 6 DOI: 10.1038/ncomms10140 Open Access Show Abstract ▼ Abstract: Diacylglycerol kinase catalyses the ATP-dependent conversion of diacylglycerol to phosphatidic acid in the plasma membrane of Escherichia coli. The small size of this integral membrane trimer, which has 121 residues per subunit, means that available protein must be used economically to craft three catalytic and substrate-binding sites centred about the membrane/cytosol interface. How nature has accomplished this extraordinary feat is revealed here in a crystal structure of the kinase captured as a ternary complex with bound lipid substrate and an ATP analogue. Residues, identified as essential for activity by mutagenesis, decorate the active site and are rationalized by the ternary structure. The γ-phosphate of the ATP analogue is positioned for direct transfer to the primary hydroxyl of the lipid whose acyl chain is in the membrane. A catalytic mechanism for this unique enzyme is proposed. The active site architecture shows clear evidence of having arisen by convergent evolution.	Dec 2015

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