PMID:11807267
| Citation |
Roujeinikova, A, Baldock, C, Simon, WJ, Gilroy, J, Baker, PJ, Stuitje, AR, Rice, DW, Rafferty, JB and Slabas, AR (2002) Crystallization and preliminary X-ray crystallographic studies on acyl-(acyl carrier protein) from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 58:330-2 |
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| Abstract |
Acyl carrier 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 P2(1)2(1)2(1), with unit-cell parameters a = 27.6, b = 41.6, c = 63.7 A. The asymmetric unit appears to contain one subunit, corresponding to a packing density of 2.1 A(3) Da(-1). Crystals of the selenomethionine-substituted (SeMet) protein were obtained using different conditions and belong to space group P6(3), with unit-cell parameters a = b = 63.4, c = 37.0 A, alpha = beta = 90, gamma = 120 degrees and with a monomer in the asymmetric unit (V(M) = 2.5 A(3) 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 P2(1)2(1)2(1) and have unit-cell parameters a = 27.3, b = 41.9, c = 64.5 A. A data set suitable for MAD phasing was collected from the crystals of the I62M variant to 1.8 A resolution on the ESRF beamline ID14-4. |
| Links | |
| Keywords |
Acyl Carrier Protein/chemistry; Acyl Carrier Protein/genetics; Crystallization; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli/genetics; Mutagenesis, Site-Directed; Protein Conformation; Selenomethionine/chemistry |
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