Serial macromolecular crystallography at ALBA Synchrotron Light Source

Martin-Garcia, J.M.; Botha, S.; Hu, H.; Jernigan, R.; Castellví, A.; Lisova, S.; Gil, F.; Calisto, B.; Crespo, I.; Roy-Chowdhury, S.; Grieco, A.; Ketawala, G.; Weierstall, U.; Spence, J.; Fromme, P.; Zatsepin, N.; Boer, D.R.; Carpena, X.

doi:10.1107/S1600577522002508

Figure 3
Quality of the 2mFo-DFc electron density maps for all structures tested contoured at 1σ. (a) Lysozyme illustrated as a blue cartoon and stick representation. Solvent molecules (water in red) and Cl⁻ ions (green) are represented as spheres. A closer view (panel below) of the Glu35 and Asp52 residues at the catalytic site. (b) Proteinase K illustrated as a pink cartoon and stick representation. Solvent molecules (water in red) and the Ca²⁺ ion (green) are represented as spheres. A closer view (panel below) of one of the Ca²⁺ ions. (c) The two phycocyanin subunits (α green and β salmon) illustrated as a blue cartoon and stick representation. The chromophores are shown in a yellow cartoon and stick representation. Solvent molecules (water in red), Na⁺ ions (purple) and Cl⁻ ions (green) are represented as spheres. A closer view (panel below) of the phycocyanobilin chromophore. (d) The α-spectrin-SH3 domain illustrated as a yellow cartoon and stick representation. Water molecules are shown as red spheres. A closer view (panel below) of the Trp41 and Trp42 residues at the binding site. (e) Hexameric human insulin illustrated as a cartoon and stick representation. The dimer in the asymmetric unit is shown in purple and symmetry-related molecules are shown in dark grey. A closer view (right panel) of the coordination of the Zn²⁺ ion (blue) with the His10 residues (sticks), and the Cl⁻ ions (in green, and black for the symmetry-related molecules).

JOURNAL OF
SYNCHROTRON
RADIATION

ISSN: 1600-5775

Volume 29| Part 3| May 2022| Pages 896-907

https://doi.org/10.1107/S1600577522002508

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