Crystallization and preliminary X-ray studies of rhamnogalacturonase A from Aspergillus aculeatus.
Recombinant rhamnogalacturonase A from Aspergillus aculeatus has been crystallized and X-ray diffraction data has been collected. Crystals were grown by the hanging-drop vapour-diffusion technique, under the conditions 10% PEG 8000, 0.05 M KH(2)PO(4) and 0.1 M sodium acetate buffered at pH 3.5. The crystals diffract beyond 2.0 A resolution and belong to one of the orthorhombic space groups I2(1)2(1)2(1) or I222, with the unit-cell parameters a = 62.9, b = 125.4 and c = 137.0 A. There is one molecule in the asymmetric unit and a solvent content of approximately 54%. The enzyme is highly glycosylated corresponding to 5.9 kDa.
Petersen
T N
TN
Centre for Crystallographic Studies, H. C. Ørsted Institute, University of Copenhagen, Denmark.
Christgau
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S
Kofod
L V
LV
Kauppinen
S
S
Johnson
A H
AH
Larsen
S
S