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Table 1 X-ray data-collection and refinement statistics

From: Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD

  SycD21-163/YopD
Data collection  
 Wavelength (Å) 0.918
 Space group P 3121
 Unit cell parameters  
  a, b, c (Å) 106.4, 106.4, 52.0
  α, β, γ (°) 90, 90, 120
 Resolution range (Å) 25–2.5 (2.64-2.5)
 No. observed/unique reflections 166476/11931
 Completeness 99.4 (97.0)
 Multiplicity 14.0 (10.0)
 R merge (%)* 10.6 (57.1)
 Mean I/σ(I) 18.5 (3.1)
 Wilson B factor (Ų) 79.6
Refinement  
 R work /R free (%)§ 19.0/23.8 (31.3/34.8)
 Mean B factor (Ų)  
  Overall 79.2
  Protein 78.1
  Peptide 84.0
  Ligand/ion 105.3
  Water 75.3
 No. of atoms  
  Protein/peptide 1127
  Ligand/ion 35
  Water 17
 R.m.s.d.  
  bond (Å) 0.007
  angle (°) 1.061
 Ramachandran  
  favored (%) 95.6
  allowed (%) 4.4
  1. * R merge = hkl i | I i ( h k l ) I ( h k l ) | / hkl i I i ( h k l ) where I i (hkl) is the i th measurement of the reflection (hkl).
  2. § R work / R free = hkl | | F obs | | F calc | | / hkl | | F obs | | . R work was calculated from the work set. R free was calculated from the test set encompassing 4.9% of the total reflections. The test set was not used in refinement. Values in parentheses belong to the highest resolution shell.