Large-Scale Production of Microcrystals and Precipitates of Proteins and Their Complexes
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 degrees 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).
P350-Microcrystals-Protein-Complexes-Chan-Huot-Duma-Charbonnier-Herbert-Pucheta-Assairi-Blouquit-Abergel-Bodenhausen-Crystal-Growth-Design-12-6199-2012.pdf
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