TY - JOUR
T1 - Large-scale production of microcrystals and precipitates of proteins and their complexes
AU - Chan-Huot, Monique
AU - Duma, Luminita
AU - Charbonnier, Jean Baptiste
AU - Herbert-Pucheta, Jose Enrique
AU - Assairi, Liliane
AU - Blouquit, Yves
AU - Abergel, Daniel
AU - Bodenhausen, Geoffrey
PY - 2012/12/5
Y1 - 2012/12/5
N2 - 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).
AB - 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).
UR - http://www.scopus.com/inward/record.url?scp=84870857311&partnerID=8YFLogxK
U2 - 10.1021/cg301378j
DO - 10.1021/cg301378j
M3 - Artículo
AN - SCOPUS:84870857311
SN - 1528-7483
VL - 12
SP - 6199
EP - 6207
JO - Crystal Growth and Design
JF - Crystal Growth and Design
IS - 12
ER -