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Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1961-4.

Purification and crystallization of precursors and autoprocessed enzymes of Flavobacterium glycosylasparaginase: an N-terminal nucleophile hydrolase.

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  • 1New England Biolabs, 32 Tozer Road, Beverly, MA 01915-5599, USA.


Glycosylasparaginase (GA) represents a novel group of proteins that are activated by self-catalyzed peptide-bond cleavage from a single-chain precursor to yield the two subunits required for hydrolase activity. The wild-type GA precursor autoproteolyzes spontaneously into alpha and beta subunits. Strategies are reported here for purification to homogeneity of GA from Flavobacterium meningosepticum in both single-chain precursor and mature (autoprocessed) forms. The recombinant proteins crystallize in different space groups: P1 and P2(1) for the precursor and mature enzymes, respectively. The precursor crystals diffract to 1.9 A resolution with laboratory X-ray radiation.

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