Fusarium oxysporum trypsin at atomic resolution at 100 and 283 K: a study of ligand binding

The X‐ray structure of F. oxysporum trypsin has been determined at atomic resolution, revealing electron density in the binding site which was interpreted as a peptide bound in the sites S1, S2 and S3. The structure, which was initially determined at 1.07 Å resolution and 283 K, has an Arg in the S1...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-01, Vol.57 (1), p.8-19
Hauptverfasser:	Rypniewski, Wojciech R., Østergaard, Peter R., Nørregaard-Madsen, Mads, Dauter, Miroslawa, Wilson, Keith S.
Format:	Artikel
Sprache:	eng
Schlagworte:	Crystallography, X-Ray Fusarium - chemistry ligand binding Ligands Models, Molecular Protein Binding Protein Structure, Secondary trypsin Trypsin - chemistry Trypsin - metabolism
Online-Zugang:	Volltext
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