Protein crystallography with a micrometre-sized synchrotron-radiation beam

For the first time, protein microcrystallography has been performed with a focused synchrotron-radiation beam of 1 µm using a goniometer with a sub-micrometre sphere of confusion. The crystal structure of xylanase II has been determined with a flux density of about 3 × 1010 photons s−1 µm−2 at the sample

Magnetic effects on fields morphologies and reversals in geodynamo simulations

International audienceThe dynamo eect is the most popular candidate to explain the non-primordial magnetic elds of astrophysical objects. Although many systematic studies of parameters have already been made to determine the dierent dynamical regimes explored by direct numerical geodynamo simulations, it is only recently that the regime corresponding to the outer core of the Earth characterized by a balance of forces between the Coriolis and Lorentz forces is accessible numerically. In most previous studies, the Lorentz force played a relatively minor role. For example, they have shown that a purely hydrodynamic parameter (the local Rossby number Ro) determines the stability domain of dynamos dominated by the axial dipole (dipolar dynamos). In this study, we show that this result cannot hold when the Lorentz force becomes dominant. We model turbulent geodynamo simulations with a strong Lorentz force by varying the important parameters over several orders of magnitude. This method enables us to question previous results and to argue on the applications of numerical dynamos in order to better understand the geodynamo problem. Strong dipolar elds considerably aect the kinetic energy distribution of convective motions which enables the maintenance of this eld conguration. The relative importance of each force depends on the spatial length scale, whereas Ro is a global output parameter which ignores the spatial dependency. We show that inertia does not induce a dipole collapse as long as the Lorentz and the Coriolis forces remain dominant at large length scales

Design of thermoresponsive elastin-like glycopolypeptides for selective lectin binding and sorting

Selective lectin binding and sorting was achieved using thermosensitive glycoconjugates derived from recombinant elastin-like polypeptides (ELPs) in simple centrifugation-precipitation assays. A recombinant ELP, (VPGXG)40, containing periodically spaced methionine residues was used to enable chemoselective post-synthetic modification via thioether alkylation using alkyne functional epoxide derivatives. The resulting sulfonium groups were selectively demethylated to give alkyne functionalized homocysteine residues, which were then reacted with azido-functionalized monosaccharides to obtain ELP glycoconjugates with periodic saccharide functionality. These modifications were also found to allow modulation of ELP temperature dependent water solubility. The multivalent ELP glycoconjugates were evaluated for specific recognition, binding and separation of the lectin Ricinus communis agglutinin (RCA120) from a complex protein mixture. RCA120 and ELP glycoconjugate interactions were evaluated using laser scanning confocal microscopy and dynamic light scattering. Due to the thermoresponsive nature of the ELP glycoconjugates, it was found that heating a mixture of galactose-functionalized ELP and RCA120 in complex media selectively yielded a phase separated pellet of ELP-RCA120 complexes. Based on these results, ELP glycoconjugates show promise as designer biopolymers for selective protein binding and sorting.Développement de squelettes polypeptidiques recombinants pour la synthèse de glycoconjugués multivalents parfaitement défini

Quantitative Side-Chain Modifications of Methionine-Containing Elastin-Like Polypeptides as a Versatile Tool to Tune Their Properties

Tuning the lower critical solution temperature (LCST) of temperature-responsive recombinant elastin-like polypeptides has usually been achieved by designing different protein sequences, in terms of amino acid composition and length, implying tedious molecular cloning steps. In the present work, we have explored the chemoselective alkylation of methionine as an easy means to modify elastin repeat side chains and easily modulate the LCST of the polypeptides. Such a versatile synthetic method shall practically be exploited to modulate any properties of recombinant polymers