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Table 4 Data collection and Refinement Statistics for Ypd1-G68Q

From: Role of the highly conserved G68 residue in the yeast phosphorelay protein Ypd1: implications for interactions between histidine phosphotransfer (HPt) and response regulator proteins

Data Collection
 Space group P3121
 Unit cell dimensions (Å, °) a = b = 76.7, c = 66.7 and α = β = 90, γ = 120
 Resolution range (Å) 38.36–1.98 (2.051–1.98)a
 Total number of reflections 100,588
 Number of unique reflections 15,936 (1400)
Average redundancy
 % completeness 97 (72)
 Rmerge (%)b 0.051
 CC1/2c 0.879
 Mean I/σI 31 (1.95)
Refinement Statistics
 Resolution Range (Å) 38.36–1.98 (2.051–1.98)
Rwork (%)d 17.8
 Rfree (%)e 20.7
 Average B-factor (Å2) 23.73
 # of Protein Atoms 1363
 # of Waters 166
 RMSD bond length (Å) 0.010
 RMSD angles (°) 1.0
Ramachandran plot (%)
  Most favored 98.78
  Additionally allowed 1.2
  Disallowed 0
  1. aValues in () are for the highest resolution shell
  2. bRmerge = Σ(I - 〈I〉)I/Σ(I), where I is the intensity measurement of a given reflection and 〈I〉 is the average intensity for multiple measurements of this reflection
  3. cHalf-set correlation coefficient CC1/2 as defined in Karplus and Diederichs [78]
  4. dRwork = Σ||Fo| - |Fc|| / Σ|Fo|, where Fo and Fc are the observed and calculated structure factors respectively
  5. eRfree was calculated with 5% of the diffraction data that were selected randomly and not used throughout refinement