A new additive for protein crystallization.
The potential usefulness of the new zwitterionic solubilizing agent, dimethyl ethylammonium propane sulfonate (NDSB195), in protein crystallization was shown using hen egg-white lysozyme. In the presence of this agent, highly diffracting crystals were obtained using ammonium sulphate as a precipitant, whereas in its absence only amorphous precipitates were obtained. The crystals possess a triclinic unit cell not previously described and diffract to a resolution of 2 A. To ascertain that the new reagent had not produced significant changes in the protein fold the structure was determined to a resolution of 2.6 A. Only minor differences were observed (notably in regions of crystal contacts) with the known tetragonal lysozyme structure (Brookhaven Protein Data Bank entry 1HEL).
Institut Laue-Langevin, Grenoble, France.
L
L
Vuillard
T
T
Rabilloud
R
R
Leberman
C
C
Berthet-Colominas
S
S
Cusack
D003460:Crystallization; D018360:Crystallography, X-Ray; D003902:Detergents; D007202:Indicators and Reagents; D015394:Molecular Structure; D009113:Muramidase / Q000737:chemistry*; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D000644:Quaternary Ammonium Compounds
D003902:Detergents; D007202:Indicators and Reagents; D011506:Proteins; D000644:Quaternary Ammonium Compounds; D009113:Muramidase