1. A Mimivirus Enzyme that Participates in Viral Entry
Thomas Klose, Dominik A. Herbst, Hanyu Zhu, Joann P. Max, Hilkka I. Kenttämaa, Michael G. Rossmann 
Structure 
Volume 23, Issue 6, Pages (June 2015)
DOI: /j.str
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2. Structure 2015 23, 1058-1065DOI: (10.1016/j.str.2015.03.023)
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3. Figure 1
Structure of R135
(A and B) Top view (A) and side view (B) of an R135 dimer, rainbow colored from blue at the N terminus to red at the C terminus.
(C and D) Top view (C) and side view (D) of an R135 dimer. Each monomer is colored in red and green, respectively.
Structure  , DOI: ( /j.str )
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4. Figure 2 Topology Diagram of R135
The FAD binding domain and the substrate recognition domain are colored in green and blue, respectively, and are separated by a black line. The FAD binding loop involved in dimer formation is shown in orange.
Structure  , DOI: ( /j.str )
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5. Figure 3
Oligomer Formation of R135 in Solution Analyzed by Sedimentation Velocity Centrifugation
The majority of R135 forms a dimer with a sedimentation coefficient of 7.8 S in solution, independent of the protein concentration.
Structure  , DOI: ( /j.str )
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6. Figure 4 FAD Cofactor and its Protein Environment
Shown are the residues involved in hydrogen bonds (depicted by dashed lines) and hydrophobic interactions with the flavin ligand. The figure was generated using the program LIGPLOT+ (Laskowski and Swindells, 2011).
Structure  , DOI: ( /j.str )
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7. Figure 5 Electron Density Surrounding the FAD Cofactor
(A and B) Model of the FAD cofactor shown from the top (A) and side (B). The 2Fo − Fc electron density map drawn at a σ level of 1.0 is shown as a mesh.
(C and D) Overlays of a planar (red) and the observed butterfly (green) conformation shown from the top (C) and side (D). The electron density map is displayed in the same way as in (A) and (B).
Structure  , DOI: ( /j.str )
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8. Figure 6 Lignin Model Dimer
Chemical structure of guaiacylglycerol-β-guaiacyl ether, the compound used in all lignin degradation assays.
Structure  , DOI: ( /j.str )
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