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. Author manuscript; available in PMC: 2020 Dec 7.
Published in final edited form as: Proteins. 2015 Apr 28;83(7):1201–1208. doi: 10.1002/prot.24804

Table I.

Data Collection and Structure Refinement Statistics

Data collection Plk2-PBD

 Space group /23
 Unit cell dimensions
  a, b, c (Å) 152.29, 152.29, 152.29
  α, β, γ (°) 90, 90, 90
 Wavelength (Å) 0.9795
 Resolution (Å) 50.0–2.7 (2.75–2.70)b
Rsyma 7.2 (35.7)
I/σ (I) 48.1 (5.1)
 Completeness (%) 99.6 (99.4)
 Redundancy 22.1 (7.9)
Refinement
 Resolution (Å) 50.0–2.7
 No. of reflections 16,221
Rworkc/Rfree 22.5/26.3
 No. atoms
  Protein 3467
  Water and ions 29
 RMS deviations
  Bond lengths (Å) 0.004
  Bond angles (°) 1.048
 Ramachandran plot (%)
  Most favored region 96.0
  Additionally allowed region 4.0
  Generously allowed region
 Average B-values (Å2)
  Protein 49.1
  Water and ions 48.3
a

Rsym=|IobsIavg|/Iobs, where Iobs is the observed intensity of individual reflection and Iavg is average over symmetry equivalents.

b

The numbers in parentheses are statistics from the highest resolution shell.

c

Rwork=Fo||Fc||/|Fo|, where |Fo| and |Fc| are the observed and calculated structure factor amplitudes, respectively. Rfree was calculated with 10% of the data.