3 results match your criteria: "UMR 5075 CNRS-CEA-Universite Joseph Fourier[Affiliation]"

Enhanced cyan fluorescent protein (ECFP) and its variant Cerulean are genetically encoded fluorophores widely used as donors in FRET-based cell imaging experiments. First, we have confirmed through denaturation experiments that the double-peak spectroscopic signature of these fluorescent proteins originates from the indole ring of the chromophore. Then, to explain the improvement in the fluorescence properties of Cerulean compared to those of ECFP, we have determined the high-resolution crystal structures of these two proteins at physiological pH and performed molecular dynamics simulations.

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Overproduction, purification and preliminary crystallographic analysis of the carbohydrate-recognition domain of human langerin.

Acta Crystallogr Sect F Struct Biol Cryst Commun

February 2008

Laboratoire des Protéines Membranaires, Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5075 CNRS/CEA/Université Joseph Fourier, 41 Rue Jules Horowitz, 38027 Grenoble CEDEX, France.

Langerin, a lectin that is specific to Langerhans cells, interacts with glycoconjugates through its carbohydrate-recognition domain (CRD). This carbohydrate binding occurs by an avidity-based mechanism that is enabled by the neck domain responsible for trimerization. Langerin binds HIV through its CRD and thus plays a protective role against its propagation by the internalization of virions in Birbeck granules.

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MAD on threonine synthase: the phasing power of oxidized selenomethionine.

Acta Crystallogr D Biol Crystallogr

September 2001

Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5075 CNRS-CEA-Université Joseph Fourier, 41 Rue Jules Horowitz, F-38027 Grenoble CEDEX 1, France.

The use of selenomethionine and anomalous dispersion has become the most widely used way of solving the phase problem for de novo protein structure determination. In this paper, MAD data collected from oxidized and reduced selenomethionine-containing protein are described, and it is shown that oxidized selenomethionine has a very strong phasing power and can be efficiently used if the oxidation is uniform. The comparison was performed on threonine synthase crystals.

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