Large-scale production of microcrystals and precipitates of proteins and their complexes

Chan-Huot M.; Duma L.; Charbonnier J.-B.Herbert-Pucheta J.-E.Assairi L.Blouquit Y.Abergel D.Bodenhausen G.

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Large-scale production of microcrystals and precipitates of proteins and their complexes

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The optimum conditions for the formation of plate-like and urchin-like microcrystals of biomolecules and their transfer to rotors for solid-state NMR spectroscopy depend on a variety of factors, of which minimizing the manipulation of the microcrystals and storing the sample for several months at 277 K (4 °C) play an important role. Three biological systems were investigated: Hen Egg-White (HEW) lysozyme (129 residues), the lengthened C-terminal domain (LCter) of Human centrin 2 (89 residues), and the complex between the C-terminal domain (Cter) of Human centrin 2 (79 residues) and the P17-XPC peptide (17 residues).

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《Crystal growth & design》 |2012年第12期|6199-6207|共9页
作者
Chan-Huot M.; Duma L.; Charbonnier J.-B.Herbert-Pucheta J.-E.Assairi L.Blouquit Y.Abergel D.Bodenhausen G.;
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作者单位

Institut Curie, 91405 Orsay, France;

Département de Chimie, Ecole Normale Supérieure, 24 rue Lhomond, 75231 Paris cedex 05, France;

UMR 8221, Laboratoire de Biologie Structurale et Radiobiologie, IBiTec-S, CEA, 91191 Gif-sur-Yvette, France;

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正文语种英语
中图分类晶体学;
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Large-scale production of microcrystals and precipitates of proteins and their complexes

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