Skip to main content
. Author manuscript; available in PMC: 2019 Mar 20.
Published in final edited form as: Biochemistry. 2018 Mar 6;57(11):1702–1710. doi: 10.1021/acs.biochem.7b01075

Table 1.

Data Collection and Refinement Statistics for the Crystal Structure of cdh23 and pcdh15(N2)

Data Collection and Refinement

 Space group C121

 Unit cell parameters:
  a, b, c (Å) 157.75, 57.79, 155.26
  α,β,γ (°) 90, 99.17, 90

 Molecules per asymmetric unit 2

 Beam source APS 24-ID-C

 Wavelength (Å) 0.97920

 Resolution limit (Å) 2.26

 Unique reflections 65061 (2736)

 Redundancy 3.2 (2.5)

 Completeness (%) 96.8 (84.9)

 Average I/σ(I) 13.4 (2.3)

 Rmerge 0.08 (0.40)

Refinement

 Resolution Range (Å) 50.0-2.26 (2.30-2.26)

 Residues (atoms) 866 (6790)

 Water molecules 463

 Rwork (%) 18.7 (28.4)

 Rfree (%) 23.3 (35.2)

 RMS deviations
  Bond lengths (Å) 0.018
  Bond angles (°) 1.806

 B-factor average
  Protein 54.3
  Ligand/ion 39.1
  Water 44.9

Ramachandran Plot Regions

 Most favored (%) 88.9

 Additionally allowed (%) 10.7

 Generously allowed (%) 0.4

 Disallowed (%) 0.0

Interface Area (Å2) 1102.3

PDB ID code 4XXW