Crystallization and preliminary X-ray diffraction studies of the heterogeneously glycosylated enzyme rhamnogalacturonan acetylesterase from Aspergillus aculeatus.
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 A) are orthorhombic. The limit of the diffraction pattern of the other (trigonal) form is 2.5 A. 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.
Centre for Crystallographic Studies, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen, Denmark.
A
A
Molgaard
J F
JF
Petersen
S
S
Kauppinen
H
H
Dalbøge
A H
AH
Johnsen
J C
JC
Navarro Poulsen
S
S
Larsen
D000115:Acetylesterase / Q000737:chemistry* / Q000302:isolation & purification; D001230:Aspergillus / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D005656:Fungal Proteins / Q000737:chemistry* / Q000302:isolation & purification; D006031:Glycosylation; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational
D005656:Fungal Proteins; C096859:rhamnogalacturonan acetylesterase; D000115:Acetylesterase