Table 2.

X-ray diffraction data and refinement statistics for GluXyn-1

Crystal data
Space group	P21
Cell axes, Å	45.27 133.70 77.95
Cell angles, °	90 99.76 90
No. of molecules per asymmetric unit	2
Data statistics*
Resolution limits, Å	20.0–2.1
Resolution limits, outer shell, Å	2.17–2.1
No. of observations	165,157
No. of unique reflections	48,499
Average multiplicity	3.4 (3.2)
Completeness, %	91.3 (80.0)
R(merge)†, %	5.8 (23.0)
〈I/σ(I)〉	11.6 (3.3)
Reflections with I ≥ 3 σ(I), %	81.6 (62.3)
Refinement and model statistics
No. of protein nonhydrogen atoms	6,219
No. of solvent molecules	312
No. of reflections	48,305
No. of reflections, test set	2,440
Degrees of freedom	26,132
R(cryst), %	17.7
R(free), %	22.4
Mean B, all protein atoms, Å2	21.2
Mean B, solvent, Å2	25.6
Ramachandran residues in most  favored regions, %	88.1
Ramachandran outliers	None
rms deviation from target values‡
Bond lengths, Å	0.012
Bond angle distances, Å	0.031
Planar 1–4 distances, Å	0.031

^*Numbers in parentheses refer to data in outer resolution shell. 

^†R(merge) = 100 × (Σ_h,i|I_h,i − I_h |/Σ_h,i I_h,i), where the summation is over all observations I_h,i contributing to the reflection intensities I_h. 

^‡With respect to the parameters of Engh and Huber (41).