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Table 1 Data collection and refinement statistics

From: Structural characterization of S100A15 reveals a novel zinc coordination site among S100 proteins and altered surface chemistry with functional implications for receptor binding

A. Data collection S100A15 S100A7D24G
Spacegroup I2 P43212
a, b, c (Å) 52.03, 33.47, 64.05 51.48, 51.48, 117.23
α, β, γ (deg.) 90, 90.81, 90 90, 90, 90
Wavelength 0.9794 0.9794
Resolution range (Å) 40.66-1.70 (1.79-1.70) 38.68-1.60 (1.69-1.60)
Measured reflections 44302 203068
Unique reflections 12285 21100
Redundancy 3.6 (3.6) 9.6 (9.8)
Completeness (%) 99.6 (100.0) 99.6 (98.4)
I/σ(I) 8.7 (2.5) 15.3 (2.6)
Rmergea 0.071 (0.385) 0.048 (0.430)
B. Refinement   
Resolution (Å) 28.15-1.70 (1.74-1.70) 34.76-1.60 (1.64-1.60)
Rcrystb 0.199 (0.313) 0.190 (0.250)
Rfreec 0.230 (0.328) 0.225 (0.274)
No. of atoms   
 Protein 767 773
 Solvent 110 148
 Calcium 1 1
 Zinc 2 1
 Chloride 1 1
B-values (Å2)   
 Protein 30.29 23.42
 Solvent 45.84 41.57
 Calcium 23.60 19.85
 Zinc 30.52 20.80
 Chloride 35.94 24.99
r.m.s.d   
 Bond lengths (Å) 0.013 0.016
 Bond angles (deg.) 1.321 1.533
Ramachandran statistics   
Most favoured 97.87 98.91
Allowed 2.13 1.09
Disallowed 0 0