4.7 Article

Large-Scale Production of Microcrystals and Precipitates of Proteins and Their Complexes

Journal

CRYSTAL GROWTH & DESIGN
Volume 12, Issue 12, Pages 6199-6207

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/cg301378j

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Funding

  1. Agence Nationale de la Recherche [ANR-09-BLAN-0111-01]
  2. network of Tres Grands Equipements de Resonance Magnetique Nucleaire a Tres Hauts Champs (TGE RMN THC), CNRS [3050]
  3. Agence Nationale de la Recherche (ANR) [ANR-09-BLAN-0111] Funding Source: Agence Nationale de la Recherche (ANR)

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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 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).

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