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Table 1 Summary of crystal parameters, data collection, and refinement statistics for Acel_2062 from acidothermus cellulolyticus 11b [PDB:3e11]

From: New mini- zincin structures provide a minimal scaffold for members of this metallopeptidase superfamily

Data collection λ 1MADSe λ 2MADSe λ 3MADSe
Wavelength (Å) 0.97949 0.91837 0.97897
Resolution range (Å) 29.437-1.800 29.412-1.801 29.399-1.803
No. of observations 49,068 49,153 48,819
No. of unique reflections 19,523 19,533 19,440
Completeness (%) 95.3 (94.6)a 95.5 (93.5)a 94.9 (90.2)a
Mean I/σ(I) 8.50 (1.69)a 8.31 (1.67)a 8.08 (1.51)a
R sym on I (%) 6.3 (48.0)a 6.4 (45.7)a 6.8 (55.5)a
R meas on I (%) 9.1 (63.8)a 9.6 (64.7)a 10.5 (74.3)a
Highest resolution shell (Å) 1.86-1.80 1.86-1.80 1.86-1.80
Model and refinement statistics
Resolution range (Å) 29.44-1.80
No. of reflections (total) 19,518
No. of reflections (test) 1,004
Completeness (%total) 99.0
Data set used in refinement λ 1 MADSe
Cutoff criteria |F| > 0
R cryst 0.175
R free § 0.204
Stereochemical parameters
Restraints (RMSD observed)  
Bond angle (°) 1.386
Bond length (Å) 0.014
Average isotropic B-value (Å2) 11.273
ESU†† based on Rfree (Å) 0.125
Protein residues/atoms 228/1791
Water/Ions 193
  1. ahighest resolution shell.
  2. R sym  = S|Ii- < Ii > |/S|Ii| where Ii is the scaled intensity of the ith measurement and < Ii > is the mean intensity for that reflection.
  3. R meas is the redundancy-independent Rsym. [18, 19].
  4. R cryst  = S| |Fobs|-|Fcalc| |/S|Fobs| where Fcalc and Fobs are the calculated and observed structure factor amplitudes, respectively.
  5. §R free  = as for R cryst , but for 4.9% of total reflections chosen at random and omitted from refinement.
  6. This value represents the total B that includes TLS and residual B components.
  7. ESU = Estimated overall coordinate error [20].
  8. Values in parentheses are for the highest resolution shell. Space group: P1211. Unit cell parameters: a = 39.03 Å b = 58.82 Å c = 46.93 α = γ = 90° β = 93.51.