CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF A BACTERIAL FLAVOHEMOGLOBIN PROTEIN

Authors
ERMLER U SIDDIQUI RA CRAMM R SCHRODER D FRIEDRICH B
Citation
U. Ermler et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF A BACTERIAL FLAVOHEMOGLOBIN PROTEIN, Proteins, 21(4), 1995, pp. 351-353
Citations number
18
Categorie Soggetti
Biology
Journal title
Proteins → ACNP
ISSN journal
08873585
Volume
21
Issue
4
Year of publication
1995
Pages
351 - 353
Database
ISI
SICI code
0887-3585(1995)21:4<351:CAPDSO>2.0.ZU;2-E
Abstract
A flavohemoglobin protein (FHP) was isolated from Alcaligenes eutrophu s and has been crystallized by vapor diffusion methods using PEG 3350 as precipitant. The crystals of the FAD- and heme-containing protein b elong to the monoclinic space group P2(1) with unit cell parameters of 52.2 Angstrom, 85.8 Angstrom, 103.9 Angstrom, and 81.8 degrees corres ponding to two molecules per asymmetric unit. The crystals diffract at least to a resolution of 2.0 Angstrom and are suitable for an X-ray s tructure analysis. (C) 1995 Wiley-Liss, Inc.