Table 1.

Data collection and structure refinement statistics

	LDAO-bound I239T/G354E	MV-bound I239T/G354E	DXC-bound I239T/G354E
Data collection
Space group	C2	C2	C2
Cell dimensions
a,b,c (Å)	95.24, 63.03, 102.34	95.07, 63.15, 102.07	93.48, 71.37, 113.14
α,β,γ (°)	90, 101.28, 90	90, 100.87, 90	90, 109.73, 90
Resolution (Å)	100.0–2.2 Å	100.0–2.8 Å	100.0–3.0 Å
Rsyma	0.08 (0.66)	0.07 (0.41)	0.04 (0.54)
CC1/2b	0.99 (0.26)	0.99 (0.68)	0.99 (0.27)
I/σ	9.5 (1.0)	12.6 (1.4)	40.0 (1.1)
Completeness (%)	92.5 (53.9)	90.4 (86.5)	98.0 (76.4)
Redundancy	2.7	4.7	14.9
Phasing
Resolution range	20.0–3.0 Å	20.0–3.5 Å	20.0–4.0 Å
Phasing powerc	1.01	1.13	1.24
Rcullisd	0.99	0.97	0.93
Figure of merite	0.23	0.27	0.34
Refinement
Resolution range	15.0–2.2 Å	15.0–2.8 Å	15.0–3.0 Å
No. reflections	26746	12656	10817
Rcrystf/Rfreeg (%)	22.2/24.8	20.4/24.2	26.9/29.3
No. atoms	3082	3007	2951
<B>protein	49	60	100
<B>ligand	50	65	98
<B>water	60	57	N.A.
r.m.s. deviations
Bond lengths (Å)	0.006	0.005	0.009
Bond angles (o)	1.0	1.0	1.2
Ramachandran
favored	99.7%	100%	99.4%
allowed	0.3%	0%	0.6%
disallowed	0%	0%	0%

^aR_sym  =  Σ| I−<I> | /ΣI, where I is the observed intensity of symmetry-related reflections

^bCC_1/2 is the half-split Pearson correlation coefficient

^cPhasing power  =  F_h / E, where F_h is the rms isomorphous/anomalous difference and E the rms residual lack-of-closure

^dR_cullis (ano) = Σ(||ΔFPH(obs)|−|ΔFPH(calc)||) / Σ|ΔFPH(obs)|, where ΔFPH(obs) and ΔFPH(calc) are the observed and calculated structure factor differences between Bijvoet pairs, respectively

^eFigure of merit is defined as weighted mean value of the cosine of phase error

^fR_cryst  = Σ(||F_obs|−|F_calc||) / Σ(|F_obs|), where F_obs and F_calc are the observed and calculated structure factors, respectively

^gR_free is the same as R_cryst but calculated with 5% of the reflections excluded from structure refinement