Identification and structural analysis of a thermophilic β-1,3-glucanase from compost

Bioresources and Bioprocessing

Table 2 Diffraction data collection and refinement statistics

Variable	X-ray 100 K
Data collection
Space group	P 2₁2₁2₁
Unit cell dimensions
a, b, c (Å)	60.4, 61.0, 70.7
α, β, γ (°)	α = β = γ = 90°
Resolution (Å)	50.00–1.14 (1.16–1.14)
Unique reflections	95,197 (4703)
Multiplicity	11.5 (8.3)
Completeness (%)	100.00 (100.00)
Wavelength (Å)	0.98
R_sym^a	0.150 (0.942)^b
< I > /σ < I >	16.6 (2.0)
Refinement
Resolution (Å)	16.93–1.14 (1.16–1.14)
R_work^c/R_free^d	0.132/0.158
No. of atoms
Protein	2221
Tris	8
Mg²⁺	1
Water molecules	297
B factors
Protein	12.29
Solvent	26.84
Deviation from ideality
Bond length (Å)	0.0136
Bond angle (°)	1.842
Ramachandran plot statistics (%)
Preferred regions	97.86
Allowed regions	2.14
Outliers	0
PDB ID code	7EO3

^aR_sym = ∑ (|Ii – < I >|)/∑(I), where Ii is the measured intensity and < I > is the mean intensity of all measured observations equivalent to reflection Ii
^bValues in parentheses are statistics from the highest-resolution shell
^cR_work = ∑||F_obs| – |F_calc||/∑|F_obs|, where |F_obs| is the observed diffraction amplitude and |F_calc| is the corresponding calculated structure factor amplitude
^dR_free is defined as R_work, which involves 5% of the measured reflections not used in refinement and set aside for cross-validation