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. Author manuscript; available in PMC: 2020 May 17.
Published in final edited form as: Biochemistry. 2018 Dec 7;57(50):6827–6837. doi: 10.1021/acs.biochem.8b00836

Table 1.

Crystallographic data collection and refinement statistics for EvdMO1 and EvdMΔO1 structures.

EvdMO1 EvdMΔO1 EvdMΔO1
Data Collection
Wavelength (Å) 0.918 0.979 0.979
Compounds added AKG, SAH AKG, SAH, fucose
Ligands modeled BTB AKG, SAH AKG, SAH
Space group I 41 2 2 P 21 P 21
a, b, c (Å) 191.6, 191.6, 269.6 51.4, 41.3, 56.5 50.2, 41.3, 58.5
 α, β, γ (deg) 90, 90, 90 90, 99.8, 90 90, 98.6, 90
Resolution (Å) 45.8 – 3.35 32.0 – 1.15 22.5 – 1.10
No. total reflections 248070 279251 421834
No. unique reflections 34942 (1759) 79855 (2893) 94601 (4550)
Completeness 96.1 (98.8) 96.3 (70.0) 98.5 (95.3)
Multiplicity 7.1 (7.1) 3.5 (2.3) 4.5 (3.7)
Wilson B factor 121.87 10.30 10.18
Mean I 31.5 (2.6) 20.2 (2.0) 23.3 (2.7)
Rsym 6.3 (92.6) 5.2 (34.7) 6.0 (43.4)
Rpim 2.4 (36.1) 3.2 (27.2) 3.1 (25.0)
CC1/2 66.9 83.6 86.8
Refinement
Rwork/Rfree (%) 22.1/26.6 15.1/17.0 13.7/15.4
No. protein atoms 9698 1952 1923
No. solvent atoms 0 322 188
No. ligand atoms 45 26 26
RMS for bonds (Å) 0.002 0.006 0.006
RMS for angles (deg) 0.57 0.984 1.009
Average B factor (Å2)
 protein 139.9 15.25 12.95
 solvent n/a 30.48 23.62
 ligand 169.1 9.95 9.66
Ramachandran plot
 favored 90.9 99.2 99.2
 allowed 8.3 0.8 0.8
 outliers 0.8 0 0
Clashscore 5.46 2.34 0.26
PDB ID 6EC3 5T38 5T39