Crystal Structure of the FAD-Containing Ferredoxin-NADP⁺ Reductase from the Plant Pathogen Xanthomonas axonopodis pv. citri

Table 1

Data collection and structural refinement statistics of XacFPR.

Data collection statistics
Space group	I222
Cell dimensions a, b, c (Å)	50.70, 99.78, 118.79
Wavelength, Å	0.99994
Resolution, Å	24.06–1.50 (1.58–1.50)
Total number of reflections	215020
Number of unique reflections	46901 (5597)
Redundancy	4.6 (2.9)
Completeness, %	96.7 (79.8)
Average 𝐼/𝜎	13.7 (1.9)
𝑅^amerge	0.057 (0.607)
Refinement statistics
Resolution range, Å	24.06–1.50
Protein nonhydrogen atoms	2072
Ligand nonhydrogen atoms	54
Solvent nonhydrogen atoms	238
𝑅^bwork (%)	20.6
𝑅^bfree (%)	22.7
r.m.s.d. bond length, Å	0.007
r.m.s.d. bond angles, °	1.316
Average B factor, Å^2
All	21.60
Protein	20.98
Ligands: FAD; Cl^−	14.25; 24.28
Waters	28.59
Ramachandran statistics
Res. in preferred regions (%)	97.64
Res. in allowed regions (%)	1.57
Res. outliers (%)	0.79

Values in parentheses correspond to the highest resolution shell.
^a𝑅_sym=∑|𝐼−𝐼_av|/∑𝐼, where the summation is over symmetry equivalent reflections.
^b𝑅_work and 𝑅_freewere calculated by the equation ∑||𝐹_obs|−|𝐹_calc||/∑|𝐹_obs|, where 𝐹_obs and 𝐹_calc are the observed and calculated structure factors, respectively. 𝑅_free was calculated for 7% of data excluded from the refinement.