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Table 2 Crystallographic data and refinement statistics

From: Structure of the S100A4/myosin-IIA complex

  S100A4Δ8C S100A4Δ8C/MIIA 1908-1923
PDB ID 4HSZ 4ETO
Source X29, BNL X4A, BNL
Wavelength (Å) 1.075 0.979
Resolution limits (Å) 46.9 – 2.25 50 – 1.54
Space group P1 P21
Unit cell (Å) a, b, c and α, β, γ (°) a = 28.80, b = 34.36, c = 95.31 and α = 95.48, β = 95.30, γ = 114.82 a = 30.28, b = 91.99, c = 32.86 and β = 112.6
Number of observations 31076 87461
Number of unique reflections 14935 24461
aCompleteness (%) 96.4 (94.1) 99.6 (100)
Mean I/σI 19.6 (2.4) 27.8 (2.76)
bRmerge on I 6.3 (42.2) 6.3 (49.6)
Bwilson2) 30.023 18.4
Refinement statistics   
Resolution limits (Å) 46.9 – 2.25 46.0 – 1.54
Number of reflections (work/free) 14159/750 23168/1247
Cutoff criteria I/σI 0 0
Protein/water atoms 2904/9 1530/86
Rwork/Rfree (5% of data) 0.228/0.277 0.209/0.251
cBonds (Å)/angles (°) 0.007/0.984 0.020/1.823
Mean B (Å2) 56.2 20.14
  1. aParentheses indicate statistics for the high–resolution data bin for x–ray and refinement data.
  2. b R merge = ∑hkli|I(hkl)i – < I(hkl) > |/∑hkli < I(hkl)i >.
  3. cValues indicate root–mean–square deviations in bond lengths, bond angles, and B-factors of bonded atoms.