Přejít k obsahu
Merck
  • The multidrug-resistance transporter MdfA from Escherichia coli: crystallization and X-ray diffraction analysis.

The multidrug-resistance transporter MdfA from Escherichia coli: crystallization and X-ray diffraction analysis.

Acta crystallographica. Section F, Structural biology communications (2017-07-12)
Kumar Nagarathinam, Frank Jaenecke, Yoshiko Nakada-Nakura, Yunhon Hotta, Kehong Liu, So Iwata, Milton T Stubbs, Norimichi Nomura, Mikio Tanabe
ANOTACE

The active efflux of antibiotics by multidrug-resistance (MDR) transporters is a major pathway of drug resistance and complicates the clinical treatment of bacterial infections. MdfA is a member of the major facilitator superfamily (MFS) from Escherichia coli and provides resistance to a wide variety of dissimilar toxic compounds, including neutral, cationic and zwitterionic substances. The 12-transmembrane-helix MdfA was expressed as a GFP-octahistidine fusion protein with a TEV protease cleavage site. Following tag removal, MdfA was purified using two chromatographic steps, complexed with a Fab fragment and further purified using size-exclusion chromatography. MdfA and MdfA-Fab complexes were subjected to both vapour-diffusion and lipidic cubic phase (LCP) crystallization techniques. Vapour-diffusion-grown crystals were of type II, with poor diffraction behaviour and weak crystal contacts. LCP lipid screening resulted in type I crystals that diffracted to 3.4 Å resolution and belonged to the hexagonal space group P6122.

MATERIÁLY
Číslo produktu
Značka
Popis produktu

Avanti
7.7 MAG, Avanti Research - A Croda Brand 850530O
Avanti
8.8 MAG, Avanti Research - A Croda Brand 850536O