Table 2.

Data collection and refinement statistics for Lhx3_LIM1+2–Isl1_LBD

	MAD data sets			Native data seta
	Peak	Remote	Inflection
Space group	C2
Unit cell parameters (Å, deg)	a=119, b=62.2, c=51.9, β=91.6
Wavelength (Å)	1.282	1.170	1.283	1.54
Resolution (Å)	2.30 (2.34–2.30)	2.30 (2.34–2.30)	2.30 (2.34–2.30)	2.05
Mosaicity (deg)	1.05	1.05	1.05	1.04
No. of unique reflections	14 610	14 313	14 339	23 109
Completeness (%)	85.4 (54.1)	83.5 (47.5)	83.7 (48.9)	96.5 (78.1)
Redundancy	6.4 (4.8)	6.1 (4.5)	6.3 (4.6)	3.5 (2.1)
Rmergeb	0.045 (0.218)	0.045 (0.243)	0.042 (0.215)	0.051 (0.388)
Average I/σ(I)	15.2 (7.0)	14.8 (6.2)	15.3 (7.3)	13.4 (2.4)
Phasing statistics
Resolution range (Å)	30–2.3
Zn sites/asymmetric unit	8
FOMMADc	0.66
FOMRESOLVEd	0.7
Model refinement
Rcryste	0.214 (0.287)
Rfreef	0.254 (0.346)
No. of reflections used in refinement	21 921
No. of reflections in the test set	1188 (5.1%)
Protein atoms (including Zn)	2377
Water molecules	48
RMSD bond length (Å)	0.02
RMSD bond angle (deg)	1.5
Mean protein B factor, all non-H atoms (Å2)	43.1
Mean water B factor (Å2)	43.5
Estimated standard uncertainties
Coordinates, based on residual R (Å)	0.2
Coordinates, based on Rfree (Å)	0.18
Ramachandran plot, residues in
Favoured regions (%)	93.9
Additional allowed regions (%)	6.1
Disallowed regions (%)	0
Values for the highest resolution shell are given in parentheses.
aNative set data from Bhati et al (2008).
bRmerge=∑h∑i∣Ii−〈I〉∣/∑h∑iIi.
cFigure of merit after SOLVE phasing.
dFigure of merit after RESOLVE.
eRcryst=∑∣∣Fobs∣−∣Fcalc∣∣/∑∣Fobs∣, where ∣Fobs∣ and ∣Fobs∣ are the observed and calculated structure factor amplitudes.
fRfree is Rcryst for the 5% validation set.