Table 1. Statistics for crystallographic structure determination
hERβ–GENrERβ–RAL
Data collection details
  Data collection siteID14‐4, ESRFX11, DESY
  Wavelength (Å)0.930.9096
  Space groupP6122P4122
  Unit cell dimensions (Å)a = b = 63.12, c = 250.23a = b = 67.55, c = 148.2
γ = 120°
Processing statistics
    Resolution range (Å)60–1.825–2.25
    Observations358 81897 187
    Unique reflections28 52316 904
    Completeness (%)99.799.0
    Rmergea4.97.7
 Outer resolution shell
    Resolution range (Å)1.83–1.802.29–2.25
    Unique reflections1370813
    Completeness (%)10098.7
    Rmergea43.346.7
  Refinement statistics
Resolution range (Å)55–1.825–2.25
Reflections used (Rfree set)27 019 (1441)15 179 (1691)
Rcryst (Rfree)b21.9 (25.5)20.4 (26.3)
Protein/ligand atoms1834/201807/34
Water molecules139128
R.m.s. bonds/angles (Å)c0.013/0.0310.014/0.038
R.m.s. backbone ΔB (2) Å d2.32.2
Mean B‐factor (Å)e41/40/43/32/4647/49/46/48/43
%A,B,L (a,b,l,p)f95.7 (4.3)95.1 (4.4)
  • a Rmerge = 100×Σ|I − <I>|/Σ<I>.

  • b Rcryst = Σ|FobsFcalc|/ΣFobs; Rfree is as Rcryst but calculated over either 5% (GEN) or 10% (RAL) of data that were excluded from the refinement process.

  • c Root mean square deviation in bond length and angle distances from Engh and Huber ideal values.

  • d Root mean square deviation between B‐factors for bonded main chain atoms.

  • e Mean temperature factor for whole molecule, main chain, side chain, ligand and water atoms, respectively.

  • f Percentage of residues located in most favoured (additional) regions of the Ramachandran plot as determined by PROCHECK (Laskowski et al., 1993).