Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS)

Marco Nardini, Stefania Spanò, Claudia Cericola, Alessandra Pesce, Gianluca Damonte, Alberto Luini, Daniela Corda, Martino Bolognesi

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)1068-1070
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume58
Issue number6 II
DOIs
Publication statusPublished - 2002

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Clinical Biochemistry
  • Structural Biology
  • Condensed Matter Physics

Fingerprint Dive into the research topics of 'Crystallization and preliminary X-ray diffraction analysis of brefeldin A-ADP ribosylated substrate (BARS)'. Together they form a unique fingerprint.

Cite this