A stepwise optimization of crystals of rhamnogalacturonan lyase from Aspergillus aculeatus.
Recombinant rhamnogalacturonan lyase from Aspergillus aculeatus has been crystallized by a stepwise procedure and X-ray diffraction data have been collected. The crystals were grown using hanging-drop vapour-diffusion and microseeding techniques. Crystals were obtained showing a flat plate morphology. The crystallization conditions were 20% PEG 4000, 9% PEG 400, 0.1 M (NH(4))(2)SO(4) and 0.1 M sodium acetate pH 4.4. These crystals diffracted to a resolution of 1.5 A. The unit-cell parameters are a = b = 77.0, c = 170.8 A with the possible space group P4(3)2(1)2 or P4(1)2(1)2. There is most likely to be one molecule in the asymmetric unit, leading to a calculated solvent content of approximately 47% for the crystals.
Centre for Crystallographic Studies, University of Copenhagen, Universitetsparken 5, DK 2100 Copenhagen, Denmark.
Renuka
R
Kadirvelraj
Pernille
P
Harris
Jens Christian N
JC
Poulsen
Sakari
S
Kauppinen
Sine
S
Larsen
D001230:Aspergillus; D003460:Crystallization; D018360:Crystallography, X-Ray; D011133:Polysaccharide-Lyases / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D011994:Recombinant Proteins; D011133:Polysaccharide-Lyases