Table 1. Data-collection and refinement statistics for the RSK2–quercitrin complex.

Data from one native crystal were used for structure determination. Values in parentheses are for the highest resolution shell.

Data collection
Space group	C2
Unit-cell parameters (Å, °)	a = 98.08, b = 40.69, c = 83.26, β = 114.3
Resolution range (Å)	30.00–1.80 (1.84–1.80)
No. of unique reflections	28004 (1389)
R merge †	0.117 (0.303)
〈I/σ(I)〉	15.2 (4.65)
Completeness (%)	99.8 (100)
Multiplicity	4.3 (3.8)
Refinement
Resolution range (Å)	25.30–1.80 (1.84–1.80)
No. of reflections	27492
R work/R free ‡	0.17/0.20
No. of atoms
Protein (non-H)	2266
Inhibitor (all atoms)	52
Water	260
B factors (Å2)
Protein	37.8
Inhibitor	29.9
Water	45.4
R.m.s. deviations
Bond lengths (Å)	0.006
Bond angles (°)	0.98

^† R _merge = , where I_i(hkl) is the intensity of the ith observation and 〈I(hkl)〉 is the mean intensity of reflection hkl.

^‡The crystallographic R factor R = ; R _free = , where all reflections belong to a test set of randomly selected data.