Literature DB >> 2671386

Crystallization of the DNA-binding Escherichia coli protein FIS.

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

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.

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Year:  1989        PMID: 2671386     DOI: 10.1016/0022-2836(89)90098-3

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  2 in total

1.  The N-terminal part of the E.coli DNA binding protein FIS is essential for stimulating site-specific DNA inversion but is not required for specific DNA binding.

Authors:  C Koch; O Ninnemann; H Fuss; R Kahmann
Journal:  Nucleic Acids Res       Date:  1991-11-11       Impact factor: 16.971

2.  The E.coli fis promoter is subject to stringent control and autoregulation.

Authors:  O Ninnemann; C Koch; R Kahmann
Journal:  EMBO J       Date:  1992-03       Impact factor: 11.598

  2 in total

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