CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF THE HETEROGENEOUSLY GLYCOSYLATED ENZYME RHAMNOGALACTURONAN ACETYLESTERASE FROMASPERGILLUS-ACULEATUS

Authors
MOLGAARD A PETERSEN JFW KAUPPINEN S DALBOGE H JOHNSEN AH POULSEN JCN LARSEN S
Citation
A. Molgaard et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF THE HETEROGENEOUSLY GLYCOSYLATED ENZYME RHAMNOGALACTURONAN ACETYLESTERASE FROMASPERGILLUS-ACULEATUS, Acta crystallographica. Section D, Biological crystallography, 54, 1998, pp. 1026-1029
Citations number
11
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biophysics,Biology
Journal title
Acta crystallographica. Section D, Biological crystallography → ACNP
ISSN journal
09074449
Volume
54
Year of publication
1998
Part
5
Pages
1026 - 1029
Database
ISI
SICI code
0907-4449(1998)54:<1026:CAPDSO>2.0.ZU;2-A
Abstract
Well diffracting crystals of rhamnogalacturonan acetylesterase from As pergillus aculeatus have been obtained in two polymorphic modification s despite its heterogeneous glycosylation. The best-diffracting crysta ls (resolution 1.55 Angstrom) are orthorhombic. The limit of the diffr action pattern of the other (trigonal) form is 2.5 Angstrom. The abili ty of the enzyme to crystallize appears to depend on the glycosylation of the protein sample. This aspect has been investigated by mass spec trometry, which also showed that the orthorhombic crystals have the sa me glycosylation as the protein sample used in the crystallization.