Table 1.

Data collection and refinement statistics of the crystal structures of the hStau1-ARF1 SBS complex and of ARF1 SBS.

Native ARF1-hStau1182–360ARF1-hStau1182–360 SeMetARF1 SBS
Data collection
 BeamlineX06DA-PXIIIX06DA-PXIIIX10SA-PXII
 Space groupP41212P41212H32
 Cell dimensions
  a, b, c (Å)105.9, 105.9, 169.2105.1, 105.1, 171.143.8, 43.8, 452.1
  α, β, γ (°)90, 90, 9090, 90, 9090, 90, 120
 Wavelength1.0450.9801.000
 Resolution (Å)50–2.89 (3.06-2.89)50–4.23 (4.48–4.23)38–1.9 (2.02–1.90)
Rsym or Rmerge0.133 (2.864)0.274 (1.685)0.089 (1.341)
II20.52 (1.32)10.81 (2.03)13.52 (1.70)
 Completeness (%)99.4 (96.8)99.7 (99.0)99.9 (99.6)
 Redundancy27.5 (25.5)27.7 (25.5.0)10.3 (10.3)
 CC (1/2)100 (81.4)100 (75.1)100 (69.5)
Refinement
 Resolution (Å)47.35–2.8938–1.9
 No. reflections40,87413,828
Rwork/Rfree21.7/24.024.4/26.2
 No. atoms4,2781,883
  Protein3,058
  RNA1,2171,828
  Water340
B-factors (A2)109.754.4
  Protein126.7
  RNA77.453.5
  Water73.246.7
 Root mean square deviations
  Bond lengths (Å)0.0040.019
  Bond angles (°)0.582.38
  • One native crystal for each construct and one SeMet crystal were used for data collection. Values in parentheses are for the highest-resolution shell.