Crystallization and preliminary X-ray diffraction studies of the heterogeneously glycosylated enzyme rhamnogalacturonan acetylesterase from Aspergillus aculeatus
Acta Crystallographica Section D
Volume 54, Issue 5, pages 1026–1029, September 1998
How to Cite
Mølgaard, A., Petersen, J. F. W., Kauppinen, S., Dalbøge, H., Johnsen, A. H., Navarro Poulsen, J.-C. and Larsen, S. (1998), Crystallization and preliminary X-ray diffraction studies of the heterogeneously glycosylated enzyme rhamnogalacturonan acetylesterase from Aspergillus aculeatus. Acta Crystallographica D, 54: 1026–1029. doi: 10.1107/S0907444998004132
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Well diffracting crystals of rhamnogalacturonan acetylesterase from Aspergillus aculeatus have been obtained in two polymorphic modifications despite its heterogeneous glycosylation. The best-diffracting crystals (resolution 1.55 Å) are orthorhombic. The limit of the diffraction pattern of the other (trigonal) form is 2.5 Å. The ability of the enzyme to crystallize appears to depend on the glycosylation of the protein sample. This aspect has been investigated by mass spectrometry, which also showed that the orthorhombic crystals have the same glycosylation as the protein sample used in the crystallization.