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

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.

authors

• Sacchettini, James

published proceedings

• J Biol Chem

author list (cited authors)

• Sacchettini, J. C., Meininger, T. A., Lowe, J. B., Gordon, J. I., & Banaszak, L. J.

citation count

• 24

complete list of authors

• Sacchettini, JC||Meininger, TA||Lowe, JB||Gordon, JI||Banaszak, LJ

publication date

• April 1987

publisher

• Elsevier  Publisher

published in

• Journal of Biological Chemistry  Journal

keywords

• Animals
• Carrier Proteins
• Crystallization
• Escherichia Coli
• Fatty Acid-binding Protein 7
• Fatty Acid-binding Proteins
• Neoplasm Proteins
• Nerve Tissue Proteins
• Rats
• X-Ray Diffraction

PubMed Central ID

• 3549720

Digital Object Identifier (DOI)

• 10.1016/s0021-9258(18)61206-2

start page

• 5428

end page

• 5430

volume

• 262

issue

• 11

URL

• http://dx.doi.org/10.1016/s0021-9258(18)61206-2