Skip to main content
. Author manuscript; available in PMC: 2017 Jan 24.
Published in final edited form as: Nat Struct Mol Biol. 2011 Dec 11;19(1):62–71. doi: 10.1038/nsmb.2169

Table 1. Data collection statistics.

Values in parentheses are for the highest resolution shell. A single crystal was used for each data set.

TRABID 245-697 AuCN TRABID 245-697
Data collection
Space group P212121 P212121
a, b, c (Å) 60.29, 72.24, 132.55 60.40, 72.15, 133.01
α, β, γ (º) 90, 90, 90 90, 90, 90
Resolution (Å) 72.2-3.50 (3.69-3.50) 44.7 - 2.23 (2.35-2.23)
Rmerge 0.193 (0.513) 0.077 (0.494)
l / σl 10.2 (5.4) 12.1 (2.7)
Completeness (%) 100 (100) 100 (100)
Redundancy 9.0 (9.2) 4.1 (4.1)
Refinement
Resolution (Å) 44.7-2.23
No. reflections 54670
Rwork / Rfree 0.202 / 0.246
No. atoms
   Protein 3433
   Ligand/ion 9
   Water 188
B-factors
   Protein 43.5
   Ligand/ion 61.5
   Water 43.2
R.m.s deviations
   Bond lengths (Å) 0.013
   Bond angles (º) 1.38