Crystallographic refinement of lignin peroxidase at 2 A.

Abstract

The crystal structure of the major lignin peroxidase isozyme from Phanerocheate chrysosporium has been Tefined to an R = 0.15 for data between 8 A and 2.03A. The refined model consists of 2 lignin peroxidase molecules in the asymmetric unit, 2 calcium ions per monomer, 1 glucosamine per monomer N-linked to Asn-257, and 476 water molecules per asymmetric unit.The model exhibits excellent geometry with a root mean square deviation fFom ideality in bond distances and angles of 0.014 A and 2.9", respectively.Molecule 1 consists of all 343 residues, while molecule 2 consists of residues 1-341.The overall root mean square deviation in backbone atoms bgtween the 2 molecules in the asymmetric unit is 0.36 A. The refinement at 2.0 A confirm! our conclusions based on the partially refined 2.