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. Author manuscript; available in PMC: 2021 Apr 1.
Published in final edited form as: Chem Biol Drug Des. 2020 Jan 20;95(4):412–426. doi: 10.1111/cbdd.13661

Table 2. Crystallization summary table.

Figures in parentheses are for the highest resolution shell. Other relevant quality indicators can be easily extracted from the PDB file header.

Refinement of data done in two steps Data processed in XDS, scaled in Aimless and used for initial refinement Data included in the final refinement after anisotropic removal of weak data (STARANISO)
Resolution (Å) 49.3 – 3.00 (3.18 –3.00) 61.7 – 2.57 (2.94 – 2.57)
Wavelength (Å) 0.97625 0.97625
Space group P31 2 1 P31 2 1
Unit cell (Å) a=b=113.8,c=79.1 a=b=113.75, c=79.2
Completeness (%) 99.6 (99.8) 55.5 (8.4)
Redundancy 3.6 (3.8) 3.6 (3.2)
No. of observations / unique reflections 43 475 / 12 088 38 750 / 10 669
<I/σ(I)> 11.6 (1.0) 13.3 (1.9)
CC(1/2) (%) 99.8 (68.8) 99.9 (69.2)
Rmerge (I) (%) 4.6 (132.0) 4.3 (68.5)
Rcryst (F) (%) 19.9 (27.4)
Rfree (F) (%) 26.6 (53.2)
No. of non-hydrogen atoms 2704
No. of water molecules 10
r.m.s. deviations from ideal geometry: Bond lengths (Å) 0.015
Bond angles (deg) 1.9
Mean B-factor protein chain, A, B (Å2) 74.0, 110.9
Mean B-factor peptide C, D (Å2) 44.0, 78.1
Mean B-factor (water, Å2) 71.7
Ramachandran plot quality#
Favored regions (%) 95.7
Allowed regions (%) 4.3
Outliers (%) 0
#

Calculated using a local Molprobity server (Chen et al., 2010).