Crystallization of the DNA-binding Escherichia coli protein FIS

H W Choe; J Labahn; S Itoh; C Koch; R Kahmann; W Saenger

doi:10.1016/0022-2836(89)90098-3

Crystallization of the DNA-binding Escherichia coli protein FIS

J Mol Biol. 1989 Jul 5;208(1):209-10. doi: 10.1016/0022-2836(89)90098-3.

Authors

H W Choe¹, J Labahn, S Itoh, C Koch, R Kahmann, W Saenger

Affiliation

¹ Institute für Kristallographie, Freie Universität Berlin, F.R.G.

PMID: 2671386
DOI: 10.1016/0022-2836(89)90098-3

Abstract

The specific DNA-binding protein FIS (factor for inversion stimulation), which stimulates site-specific DNA inversion by interaction with an enhancer sequence, was purified from an Escherichia coli strain overproducing the protein. FIS was crystallized at room temperature by microdialysis against 1.2 to 1.5 M-sodium/potassium phosphate containing 10 mM-Tris.HCl, 0.5 to 1 M-NaCl and 1 mM-NaN3 at pH 8.0 to 8.2. The crystals are stout prisms and suitable for X-ray diffraction study beyond 2.5 A resolution. They belong to the orthorhombic space group P2(1)2(1)2(1). The unit cell has dimensions a = 47.57(4) A, b = 51.13(4) A, c = 79.83(6) A and contains one FIS dimer in the asymmetric unit.

Publication types

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

MeSH terms

Bacterial Proteins*
Carrier Proteins*
Crystallization
DNA-Binding Proteins*
Escherichia coli
Escherichia coli Proteins*
Factor For Inversion Stimulation Protein
Integration Host Factors
X-Ray Diffraction

Substances

Bacterial Proteins
Carrier Proteins
DNA-Binding Proteins
Escherichia coli Proteins
Factor For Inversion Stimulation Protein
Integration Host Factors
integration host factor, E coli