Crystallization and preliminary crystallographic analysis of two endo-beta-N-acetylglucosaminidases, endo H and endo F1.
Endo H and F1 are endoglycosidases that cleave the oligosaccharide moiety of asparagine-linked glycoproteins by hydrolysis of the glycosidic bond in the N,N'-diacetylchitobiose core. The two enzymes are specific for high-mannose oligosaccharides. Here, we report the crystallization and preliminary crystallographic analysis of Endo H and Endo F1. Crystals were grown by hanging drop vapor diffusion methods. Both proteins crystallize from crystallization buffers containing polyethyleneglycol 8000 and zinc acetate as precipitating agents in cacodylate buffer. The crystals of Endo H belong to the tetragonal space group P4(1)2(1)2 (or P4(3)2(1)2) with cell dimensions: a = 85.22 A, c = 89.41 A. The crystals of Endo F1 belong to the hexagonal space group P6(1) (or P6(5)) with cell dimensions: a = 70.61 A, c = 100.32 A. Crystals of both proteins diffract to at least 1.8 A resolution.
Van Roey
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P
Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509.
Silva
G H
GH
Rao
V
V
Plummer
T H
TH
Tarentino
A L
AL
Guan
C
C
D002240:Carbohydrate Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D005417:Flavobacterium / Q000201:enzymology; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase / Q000737:chemistry*; D008969:Molecular Sequence Data
D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase