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Figure 4
Electron density near the active site of SpRub. (a) 2Fobs − Fcalc electron-density map (grey) showing the quality of the map at the active site of the protein. The labile carbamate form of Lys201L is clearly visible and has continuous electron density between the covalently bound CO2 and the lysine side chain. The active-site Mg2+ ion shows identical ligands and water-molecule coordination to earlier structures of RuBisCO, but with an additional ordered water molecule on the outskirts of this water cluster (the density is contoured at 1.2σ). (b) Fobs − Fcalc residual electron-density map (forest green) showing residual, semi-continuous electron density near the disordered region from residues 333L to 337L. However, it was not possible to model this section into this density and there may be multiple conformations that overlap with each other in this region (the density is contoured at 2.5σ).

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 80| Part 6| June 2024| Pages 117-124
https://doi.org/10.1107/S2053230X24004643
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