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. Author manuscript; available in PMC: 2017 Apr 10.
Published in final edited form as: Nat Struct Mol Biol. 2016 Aug 29;23(10):933–940. doi: 10.1038/nsmb.3284

Table 1.

Data collection and refinement statistics

DDB1-DCAF-UNG2-Vpr
(PDB: 5JK7)
DDB1-DCAF-UNG2-Vpr
(N/A)c
Data collection
Space group P1 P1
Cell dimensions
a, b, c (Å) 119.90, 128.20, 129.20 119.80, 127.00, 127.00
α, β, γ (°) 75.11, 89.44, 65.37 75.10, 89.50, 65.50
Resolution (Å) 40-3.49 40-3.99
Rmerge 14.9 (262) 8.7 (83.2)
Rpim 6.4 (115) 6.1 (55.6)
I/σ (I) 7.8 (0.7) 7.5 (1.4)
CC1/2 99.3 (24.8) 99.8 (60.1)
Completeness (%) 90.6 (40.3) 88.2 (85.8)
Redundancy 6.6 (6.2) 2.2 (2.2)
Refinement
Resolution (Å) 40-3.49
No. reflections 77,315
Rwork / Rfree 17.6 / 20.6
No. atoms
 Protein 27,701
B factors
 Protein 193.89
R.m.s. deviations
 Bond lengths (Å) 0.01
 Bond angles (°) 1.34
a

Numbers in parentheses correspond to the highest resolution shell (3.68–3.49 Å and 4.09–3.99 Å, respectively).

b

Resolution limits were extended to include weak intensity data59.

c

This data set was only used for obtaining the initial molecular replacement model.