Crystals of acylpeptide hydrolase suitable for structure determination have been obtained. This enzyme removes the N-terminal formyl or acetyl group together with the first amino acid residue from N-terminal blocked peptides including bioactive peptides. One set of crystals, which diffract to 2.2 Å, are in space group P2 with cell dimensions a = 118.6 Å, b = 82.3 Å, c = 182.1 Å, ? = 91.6°. The search for suitable heavy-atom derivatives is underway.
Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase
Scaloni A;
1993
Abstract
Crystals of acylpeptide hydrolase suitable for structure determination have been obtained. This enzyme removes the N-terminal formyl or acetyl group together with the first amino acid residue from N-terminal blocked peptides including bioactive peptides. One set of crystals, which diffract to 2.2 Å, are in space group P2 with cell dimensions a = 118.6 Å, b = 82.3 Å, c = 182.1 Å, ? = 91.6°. The search for suitable heavy-atom derivatives is underway.File in questo prodotto:
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Descrizione: Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase.
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