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Instruments / Technical Area	Publication Details	Published	Actions
I11-High Resolution Powder Diffraction	Tuning the structural and optoelectronic properties of Cs2AgBiBr6 double‐perovskite single crystals through alkali‐metal substitution Masoumeh Keshavarz , Elke Debroye , Martin Ottesen , Cristina Martin , Heng Zhang , Eduard Fron , Robert Küchler , Julian A. Steele , Martin Bremholm , Joris Van De Vondel , Hai I. Wang , Mischa Bonn , Maarten B. J. Roeffaers , Steffen Wiedmann , Johan Hofkens Advanced Materials DOI: 10.1002/adma.202001878 Diamond Proposal Number(s): [22020] Open Access Show Abstract ▼ Abstract: Lead‐free double perovskites have great potential as stable and nontoxic optoelectronic materials. Recently, Cs2AgBiBr6 has emerged as a promising material, with suboptimal photon‐to‐charge carrier conversion efficiency, yet well suited for high‐energy photon‐detection applications. Here, the optoelectronic and structural properties of pure Cs2AgBiBr6 and alkali‐metal‐substituted (Cs1−xYx)2AgBiBr6 (Y: Rb+, K+, Na+; x = 0.02) single crystals are investigated. Strikingly, alkali‐substitution entails a tunability to the material system in its response to X‐rays and structural properties that is most strongly revealed in Rb‐substituted compounds whose X‐ray sensitivity outperforms other double‐perovskite‐based devices reported. While the fundamental nature and magnitude of the bandgap remains unchanged, the alkali‐substituted materials exhibit a threefold boost in their fundamental carrier recombination lifetime at room temperature. Moreover, an enhanced electron–acoustic phonon scattering is found compared to Cs2AgBiBr6. The study thus paves the way for employing cation substitution to tune the properties of double perovskites toward a new material platform for optoelectronics.	Aug 2020
I24-Microfocus Macromolecular Crystallography	Phosphorylation decelerates conformational dynamics in bacterial translation elongation factors Ariel Talavera , Jelle Hendrix , Wim Versees , Dukas Jurėnas , Katleen Van Nerom , Niels Vandenberk , Ranjan Kumar Singh , Albert Konijnenberg , Steven De Gieter , Daniel Castro-Roa , Anders Barth , Henri De Greve , Frank Sobott , Johan Hofkens , Nikolay Zenkin , Remy Loris , Abel Garcia-Pino Science Advances 4 DOI: 10.1126/sciadv.aap9714 Diamond Proposal Number(s): [17150] Open Access Show Abstract ▼ Abstract: Bacterial protein synthesis is intricately connected to metabolic rate. One of the ways in which bacteria respond to environmental stress is through posttranslational modifications of translation factors. Translation elongation factor Tu (EF-Tu) is methylated and phosphorylated in response to nutrient starvation upon entering stationary phase, and its phosphorylation is a crucial step in the pathway toward sporulation. We analyze how phosphorylation leads to inactivation of Escherichia coli EF-Tu. We provide structural and biophysical evidence that phosphorylation of EF-Tu at T382 acts as an efficient switch that turns off protein synthesis by decoupling nucleotide binding from the EF-Tu conformational cycle. Direct modifications of the EF-Tu switch I region or modifications in other regions stabilizing the β-hairpin state of switch I result in an effective allosteric trap that restricts the normal dynamics of EF-Tu and enables the evasion of the control exerted by nucleotides on G proteins. These results highlight stabilization of a phosphorylation-induced conformational trap as an essential mechanism for phosphoregulation of bacterial translation and metabolism. We propose that this mechanism may lead to the multisite phosphorylation state observed during dormancy and stationary phase.	Mar 2018

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