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

Table 1 Data collection and refinement statistics

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-merge^b (%)	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-free^c (%)	18.77 (25.10)/22.80 (27.98)	27.43 (33.62)/32.48 (43.45)
Number of non-hydrogen atoms^d	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

PDB Protein Data Bank, RMS Root Mean Square deviation from ideal values (crystallography)
^aStatistics for the highest-resolution shell are shown in parentheses
^bR_merge = 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
^cR_factor = 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.
^dPer asymmetric unit

ISSN: 1741-7007