Crystallization of rat intestinal fatty acid binding protein. Preliminary X-ray data obtained from protein expressed in Escherichia coli. | Academic Article individual record
abstract

Rat intestinal fatty acid binding protein has been expressed in Escherichia coli, purified with bound long chain fatty acids and crystals grown from solutions of polyethylene glycol 4000. The crystals are monoclinic, space group P2(1), a = 3638 A, b = 57.2 A, c = 31.9 A, and beta = 113.9 degrees. Each unit cell contains two monomers of this 132-residue, 15.1-kDa polypeptide. The crystals are remarkably resistant to x-ray damage. X-ray diffraction data have been observed to 2.0 A resolution. Platinum chloride was used to generate a potential isomorphous heavy atom derivative.

author list (cited authors)
Sacchettini, J. C., Meininger, T. A., Lowe, J. B., Gordon, J. I., & Banaszak, L. J.
publication date
1987
keywords
  • Escherichia Coli
  • Nerve Tissue Proteins
  • X-Ray Diffraction
  • Neoplasm Proteins
  • Carrier Proteins
  • Animals
  • Fatty Acid-binding Proteins
  • Crystallization
  • Fatty Acid-binding Protein 7
  • Rats
citation count

14