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. Author manuscript; available in PMC: 2012 Jan 1.
Published in final edited form as: Nat Struct Mol Biol. 2011 Oct 9;18(11):1204–1210. doi: 10.1038/nsmb.2139

Table 1.

Data collection and refinement statistics

Human LRP6-E1E2 Human LRP6-E3E4 Human LRP6- E3E4/Dkk1c
Data collection
Space group P21 P212121 P212121
Cell dimensions
a, b, c (Å) 70.54, 144.51, 70.76 68.6, 83.75, 166.62 92.97, 104.76, 158.8
α, β, γ (°) 90, 96.0, 90 90, 90, 90 90, 90, 90
Resolution (Å) 30–2.8(2.95–2.8) 30–2.8(2.95–2.8) 30–3.1(3.21–3.1)
Rsym 9.1(33.5) 9.7(41.3) 11.4(62)
II 7(2.3) 4.8(1.8) 11(1.7)
Completeness (%) 100(100) 99.9(100) 98.4(92.8)
Redundancy 3.9(4.0) 6.8(7.1) 3.3(2.9)
Refinement
Resolution (Å) 30–2.8 30–2.8 30–3.1
No. reflections 32951 23097 27740
Rwork/Rfree 24.4/30.2 25.2/27.9 24.3/29.2
No. atoms
 Protein 9336 4833 10178
 Ligand/ion 70 70
B-factors
 Protein 70.04 91.9 87.1
 Ligand/ion 137.2 138.4
R.m.s. deviations
 Bond lengths (Å) 0.0085 0.006 0.007
 Bond angles (°) 1.21 1.1 1.08

One crystal was used for each dataset. Values in parentheses are for highest-resolution shell.