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. 2008 Aug 8;105(33):11748–11753. doi: 10.1073/pnas.0805852105

Table 1.

Crystallographic data and refinement statistics

Profilin–actin–VASP202–244 Gelsolin–actin Gelsolin–pY53–actin
Space group P212121 C2 C2
Unit cell a/b/c, Å 38.04/76.18/180.82 178.88/69.17/56.56 178.42/69.05/56.54
Unit cell α/β/γ, ° 90/90/90 90/104.36/90 90/104.2/90
Resolution, Å 2.3–50 (2.3–2.38) 1.6–50 (1.6–1.66) 1.7–50 (1.7–1.76)
Completeness, % 89.7 (80.9) 96.8 (78.4) 94.9(57.9)
Multiplicity 11.0 (11.1) 7.3 (3.8) 8.0 (2.1)
Rsym, %* 11.7 (34.9) 7.1 (52.1) 8.4 (40.7)
I/σ 20.3 (15.8) 36.6 (2.1) 23.1 (2.2)
Rfactor, % 15.7 15.0 14.1
Rfree, % 22.7 19.7 19.1
rms bonds, Å 0.015 0.011 0.012
rms angles, ° 1.504 1.326 1.365
B-factor actin/ABP, Å2 22.54/20.40 24.88/23.21 29.40/30.32
B-factor solvent, Å2 22.89 38.60 44.71
Number of aa/waters 513/318 491/461 494/460
PDB code 3CHW 3CIP 3CI5

Values in parentheses correspond to highest resolution shell.

*Rsym = Σ(I− 〈I〉)/ΣsI; I and 〈I〉, intensity and mean intensity of a reflection.

Rfactor = Σ|FoFc|/Σ|Fo|; Fo and Fc, observed and calculated structure factors.

Rfree; Rfactor of 5% of the reflections that were not used in refinement.