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Table 1 Data collection and refinement statistics

From: The pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE-family alpha pore-forming toxins

PDB code Cry6Aa trypsin-cleaved 5KUC Full-length Cry6Aa 5KUD
Data collection
 Wavelength (Å) 1.12675 0.9786
 Resolution range (Å) 50.00–2.00 (2.07–2.00)a 50.00–2.70 (2.80–2.70)
 Space group P 65 P 21 21 2
 Cell dimensions
a, b, c (Å) 112.967, 112.967, 76.627 50.367, 71.735, 142.913
 α, β, γ (°) 90.0, 90.0, 120.0 90.0, 90.0, 90.0
 Total reflections 135,786 97,894
 Unique reflections 37,186 (3343) 14,755 (1454)
 Multiplicity 3.7 (2.3) 6.6 (7.1)
 Completeness (%) 98.80 (89.40) 99.50 (100.00)
 < I>/sigma(I) 33.41 (4.51) 10.98 (2.88)
 R-mergeb (%) 6.1 (22.9) 14.6 (89.4)
Refinement
 Resolution range (Å) 30.01–2.00 (2.06–2.00) 29.14–2.70 (2.80–2.70)
 R-work/R-freec (%) 18.77 (25.10)/22.80 (27.98) 27.43 (33.62)/32.48 (43.45)
 Number of non-hydrogen atomsd 3605 3027
  protein 3183 3006
  ligand 0 0
  water 422 21
 Protein residues 402 393
 RMS, bonds (Å) 0.009 0.013
 RMS, angles (°) 1.071 1.650
 Ramachandran favored (%) 98.74 97.93
 Ramachandran outliers (%) 0.25 0.26
 Average B-factor 30.70 84.00
  1. PDB Protein Data Bank, RMS Root Mean Square deviation from ideal values (crystallography)
  2. aStatistics for the highest-resolution shell are shown in parentheses
  3. bRmerge = 100Σ(h)Σ(i)|I(i)-<I>|/ Σ(h)Σ(i)I(i) where I(i) is the ith intensity measurement of reflection h, and <I> is the average intensity from multiple observations
  4. cRfactor = Σ||F obs|-|F calc||/ Σ|F obs|. Where F obs and F calc are the structure factor amplitudes from the data and the model, respectively. To calculate R-free values, 5 % and 10 % reflections were used for Cry6Aa trypsin core and full-length Cry6Aa structures, respectively.
  5. dPer asymmetric unit