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. 2012 Sep 22;68(Pt 10):1149–1152. doi: 10.1107/S1744309112035191

Table 2. X-ray data-collection and refinement statistics for MmIMPase 1 and HsIMPase 1.

Values in parentheses are for the highest resolution shell.

  MmIMPase 1 HsIMPase 1
Space group P21 P212121
Unit-cell parameters (Å, °) a = 86.78, b = 81.49, c = 97.14, β = 133.7 a = 60.68, b = 76.05, c = 118.09
Temperature (K) 100 100
X-ray source I04-1, Diamond Light Source ID23-EH1, ESRF
Detector Pilatus 2M ADSC Q315r
Resolution (Å) 43.34–2.43 (2.56–2.43) 47.43–1.70 (1.79–1.70)
R merge (%) 0.091 (0.503) 0.047 (0.442)
No. of unique reflections 46562 (6638) 60344 (8763)
Completeness (%) 98.8 (96.7) 99.3 (100.0)
Average multiplicity 6.3 (6.0) 4.7 (4.8)
I/σ(I)〉 16.4 (3.2) 17.1 (3.5)
Refinement
R work 0.163 0.154
R free 0.214 0.186
 Mean B value (Å2) 41.84 33.14
 R.m.s.d. from ideal geometry
  Bond lengths (Å) 0.01 0.01
  Bond angles (Å) 1.24 1.12
 No. of refined atoms
  Protein 8377 4309
  Heterogen 75 58
  Solvent 848 596
 Estimated coordinate error (Luzzati) (Å) 0.258 0.213
 Ramachandran
  Favoured (%) 98.44 98.9
  Allowed (%) 1.19 1.1