Cloning, purification, crystallization and preliminary X-ray diffraction of the OleC protein from Stenotrophomonas maltophilia involved in head-to-head hydrocarbon biosynthesis

Janice A Frias; Brandon R Goblirsch; Lawrence P Wackett; Carrie M Wilmot

doi:10.1107/S1744309110031751

Cloning, purification, crystallization and preliminary X-ray diffraction of the OleC protein from Stenotrophomonas maltophilia involved in head-to-head hydrocarbon biosynthesis

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Sep 1;66(Pt 9):1108-10. doi: 10.1107/S1744309110031751. Epub 2010 Aug 28.

Authors

Janice A Frias¹, Brandon R Goblirsch, Lawrence P Wackett, Carrie M Wilmot

Affiliation

¹ University of Minnesota, Minneapolis, MN, USA.

Abstract

OleC, a biosynthetic enzyme involved in microbial hydrocarbon biosynthesis, has been crystallized. Synchrotron X-ray diffraction data have been collected to 3.4 A resolution. The crystals belonged to space group P3(1)21 or P3(2)21, with unit-cell parameters a=b=98.8, c=141.0 A.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Acyltransferases / chemistry*
Cloning, Molecular
Crystallization
Crystallography, X-Ray
Stenotrophomonas maltophilia / enzymology*

Substances

Acyltransferases
acyl protein synthetase

Abstract

Publication types

MeSH terms

Substances

Grants and funding