Crystallization and preliminary X-ray crystallographic studies on acyl-(acyl carrier protein) from Escherichia coli

Anna Roujeinikova, Clair Baldock, William J. Simon, John Gilroy, Patrick J. Baker, Antoine R. Stuitje, David W. Rice, John B. Rafferty, Antoni R. Slabas

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8 Citations (Scopus)


Acyl cartier proteins carry the lipid substrate to the enzymes of the fatty acid synthase system. Crystals of Escherichia coli acyl carrier protein to which a butyryl group has been attached via a thioester link to the phosphopantetheine prosthetic arm have been obtained by the hanging-drop vapour-diffusion method. These crystals belong to space group P212121, with unit-cell parameters a = 27.6, b = 41.6, c = 63.7 Å. The asymmetric unit appears to contain one subunit, corresponding to a packing density of 2.1 Å3 Da-1. Crystals of the selenomethionine-substituted (SeMet) protein were obtained using different conditions and belong to space group P63, with unit-cell parameters a = b = 63.4, c = 37.0 Å, α = β = 90, γ = 120° and with a monomer in the asymmetric unit (VM = 2.5 Å3 Da-1). Crystals of a SeMet butyryl-ACP I62M variant were obtained using the conditions for the native protein. Like the native crystals, these belong to space group P212121 and have unit-cell parameters a = 27.3, b = 41.9, c = 64.5 Å. A data set suitable for MAD phasing was collected from the crystals of the I62M variant to 1.8 Å resolution on the ESRF beamline ID14-4.

Original languageEnglish
Pages (from-to)330-332
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Issue number2
Publication statusPublished - 2002
Externally publishedYes

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