Crystallization and preliminary X-ray diffraction studies of a peroxidase from barley grain

A Henriksen; J F Petersen; A Svensson; J Hejgaard; K G Welinder; M Gajhede

doi:10.1016/0022-2836(92)90851-a

Crystallization and preliminary X-ray diffraction studies of a peroxidase from barley grain

J Mol Biol. 1992 Nov 20;228(2):690-2. doi: 10.1016/0022-2836(92)90851-a.

Authors

A Henriksen¹, J F Petersen, A Svensson, J Hejgaard, K G Welinder, M Gajhede

Affiliation

¹ Chemical Lab. IV, H. C. Orsted Institute, University of Copenhagen, Denmark.

PMID: 1333535
DOI: 10.1016/0022-2836(92)90851-a

Abstract

Crystals suitable for X-ray diffraction analysis of both glycosylated and non-glycosylated forms of a barley peroxidase have been grown. The crystals of the glycosylated peroxidase have been grown by the hanging drop vapour diffusion method using polyethylene glycol 4000 as the precipitant in the presence of n-propanol and potassium iodide at pH 8.5. The crystals are needles belonging to the orthorhombic spacegroup P2(1)2(1)2(1) with unit cell dimensions a = 62.95 A, b = 66.24 A and c = 70.78 A. There is one barley peroxidase molecule in the asymmetric unit. The crystals contain approximately 38% solvent and appear to be stable to lengthy X-ray exposure. They diffract to beyond 1.9 A.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Crystallization
Hordeum / enzymology*
Peroxidase / chemistry*
X-Ray Diffraction

Substances

Peroxidase