CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF PTIDE-N-4-(N-ACETYL-BETA-D-GLUCOSAMINYL)ASPARAGINE AMIDASE PNGASE-F

Authors
KUHN P TARENTINO AL PLUMMER TH VANROEY P
Citation
P. Kuhn et al., CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF PTIDE-N-4-(N-ACETYL-BETA-D-GLUCOSAMINYL)ASPARAGINE AMIDASE PNGASE-F, Journal of Molecular Biology, 241(4), 1994, pp. 622-623
Citations number
7
Categorie Soggetti
Biology
Journal title
Journal of Molecular Biology → ACNP
ISSN journal
00222836
Volume
241
Issue
4
Year of publication
1994
Pages
622 - 623
Database
ISI
SICI code
0022-2836(1994)241:4<622:CAPCAO>2.0.ZU;2-A
Abstract
PNGase F is an amidase that hydrolyzes the beta-aspartylglucosylamine bond of asparagine-linked glycopeptides and glycoproteins. Enzymatic a ctivity of PNGase F requires the recognition of both the peptide and t he carbohydrate moiety. Crystals of PNGase F were grown by sitting dro p vapor diffusion methods at 10 degrees C. The precipitating buffer co ntains both polyethylene glycol 3350 and (NH4)(2)SO4 in sodium acetate buffer at pH 4.3. The crystals belong to the orthorhombic space group C222(1) with cell dimensions: a = 87.16 Angstrom, b = 125.10 Angstrom , c = 79.33 Angstrom and diffract to 1.8 Angstrom resolution.