Molgaard A, Petersen J F, Kauppinen S, Dalbøge H, Johnsen A H, Navarro Poulsen J C, Larsen S
Centre for Crystallographic Studies, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen, Denmark.
Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):1026-9. doi: 10.1107/s0907444998004132.
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.
尽管来自棘孢曲霉的鼠李半乳糖醛酸乙酰酯酶存在异质性糖基化，但仍获得了两种多晶型修饰的衍射良好的晶体。衍射效果最佳的晶体（分辨率为1.55 Å）为正交晶系。另一种（三角晶系）形式的衍射图谱极限为2.5 Å。该酶的结晶能力似乎取决于蛋白质样品的糖基化。这一方面已通过质谱法进行了研究，质谱法还表明正交晶系晶体与结晶所用蛋白质样品具有相同的糖基化。
