Table 1. Data-collection and refinement statistics.

Values in parentheses are for the outer resolution shell.

Data-processing statistics
Wavelength (Å)	1.0332
Space group	P1
Unit-cell parameters (Å, °)	a = 48.79, b = 63.84, c = 163.89, α = 100.67, β = 90.13, γ = 103.49
No. of molecules in asymmetric unit	8
Solvent content (%)	57
Resolution range (Å)	80.4–3.20 (3.37–3.20)
No. of observations	114089
No. of unique reflections	30145
Average multiplicity	3.8 (3.9)
Completeness (%)	96.8 (98.4)
Wilson B factor (Å2)	61.5
〈I/σ(I)〉	3.4 (1.30)
R p.i.m. †	0.201 (0.547)
Refinement statistics
Resolution range (Å)	80.4–3.20
Total No. of reflections	30144
No. of working reflections	28621
No. of test reflections	1523
R xpct ‡	0.233
R free §	0.266
No. of atoms
Total	11158
Protein	10914
Carbohydrate	244
R.m.s. bond-length deviation (Å)	0.007
R.m.s. bond-angle deviation (°)	0.90
Mean B factor (Å2)
Overall	79.3
Main chain	74.8
Side chain	83.8
Carbohydrate	99.5
R.m.s. backbone B-factor deviation¶	2.2
Ramachandran statistics†† (%)
Favoured	95.4
Allowed	99.8
Outliers	0.2

^† R _p.i.m. (the precision-indicating merging R factor) = (Weiss, 2001 ▶).

^‡ R _xpct = , where |F _obs| and |F _xpct| are the observed structure-factor amplitude and the expectation of the model structure-factor amplitude, respectively (Blanc et al., 2004 ▶).

^§ R _free equals the R _xpct of the test set (5% of the data that were removed prior to refinement).

^¶R.m.s. deviation between B factors for bonded main-chain atoms.

^††As defined by MolProbity (Chen et al., 2010 ▶).