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Figure 1
Overall structure of MtDPPS. (a) The two monomers in the asymmetric unit of the MtDPPS crystal are shown as ribbon diagrams. The β-strands are named A–F and the α-helices are numbered 1–7 from the N-terminus to the C-terminus. They are coloured yellow/red for one subunit and magenta/cyan for the other subunit. The surface of the N-terminal module is shown as a grey mesh. (b) The FoFc map calculated by omitting the bound GSPP, ISPP (magenta sticks) and Mg2+ (purple sphere) as well as the associated water molecules (red spheres) and the side chains of Asp76 and Arg292 (green and orange sticks) is contoured at 3σ and 5σ levels and shown as grey and blue mesh, respectively. (c) The FoFc map calculated by omitting the bound GSPP (yellow sticks) and the side chains of Asp76 and Arg292 (orange and green sticks) is contoured at 3σ and 5σ.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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