Abstract
Brefeldin A-ADP ribosylated substrate (BARS) is a newly discovered enzyme involved in membrane fission, catalyzing the formation of phosphatidic acid by transfer of an acyl group from acyl-CoA to lysophosphatidic acid. A truncated form of BARS, lacking the C-terminal segment expected to interact with the Golgi membrane, has been expressed in soluble form in Escherichia coli, purified and crystallized. BARS crystals diffract up to 2.5 Å resolution using synchrotron radiation and belong to space group P6222/P6422, with unit-cell parameters a = b = 89.2, c = 162.6 Å, α = β = 90, γ = 120° and one molecule (39.5 kDa) per asymmetric unit. SeMet-substituted BARS has been crystallized under growth conditions very similar to those of the native protein.
Original language | English |
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Pages (from-to) | 1068-1070 |
Number of pages | 3 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 58 |
Issue number | 6 II |
DOIs | |
Publication status | Published - 2002 |
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
- Clinical Biochemistry
- Structural Biology
- Condensed Matter Physics