Table 1.

Data Collection and Refinement Statistics

Crystal	Apo-0 (NΔ33 Ddn)a	Apo-1 (NΔ30 Ddn)	Apo-2 (NΔ33 Ddn)	Holo-1 (NΔ40 Ddn + F420-ox)	Holo-2 (NΔ40 Ddn + F420-ox)	nfa33440 (+F420-ox)	nfa18080 (+F420-ox)
PDB ID code		3R5L	3R5P	3R5R	3R5W	3R5Y	3R5Z
Data Collection
Space group	C2221	C2221	P3221	C2	P21	P43	P21
Cell dimensions
a, b, c (Å)	67.37, 71.01, 50.74	67.17, 71.04, 50.53	96.18, 96.18, 33.70	146.95, 91.71, 86.50	85.34, 89.42, 127.68	71.96, 71.96, 115.47	39.70, 56.94, 66.00
α, β, γ (°)	90, 90, 90	90, 90, 90	90, 90, 120	90, 119.53, 90	90, 96.29, 90	90, 90, 90	90, 105.52, 90
Resolution (Å)b	50–1.75 (1.81–1.75)	50–1.55 (1.61–1.55)	50–1.85 (1.92–1.85)	50–2.10 (2.18–2.10)	50–1.80 (1.86–1.80)	50–1.80 (1.86–1.80)	50–1.50 (1.55–1.50)
Rmergeb	8.8 (42.5)	9.8 (62.6)	11.3 (57.2)	11.2 (47.3)	7.3 (72.2)	8.8 (66.5)	8.0 (47.3)
I/σb	54.6 (5.7)	27.5 (2.5)	12.4 (1.2)	10.7 (1.9)	22.9 (1.6)	28.2 (1.9)	18.0 (1.6)
Complete (%)b	99.1 (91.0)	97.7 (99.5)	97.9 (81.6)	97.9 (98.1)	97.5 (96.3)	100 (100)	93.5 (82.1)
Redundancyb	20.6 (18.8)	3.9 (3.3)	5.1 (3.6)	2.4 (2.5)	3.1 (3.2)	5.4 (5.4)	2.3 (1.8)
Phasing
Number found	2
Figure of merit	0.35
Refinement
Resolution (Å)		35.52–1.55	41.64–1.85	46.67–2.10	42.17–1.80	45.03–1.80	37.52–1.50
Number of reflections		16,624	14,350	53,828	159,341	51,143	38,957
Rwork/Rfree		18.0/21.1	17.1/20.3	22.7/26.3	17.3/20.6	17.3/21.4	16.6/19.2
Number of atoms
Protein		942	927	4,465	8,790	4,435	2,261
F420 (and other)		12 (MES)	10 (SO42−)	265	530	212	111 (SO42−)
Water		120	108	438	1,280	486	241
B factors (Å2)c		24.61	24.63	22.94	31.01	29.37	21.34
Rmsds
Bond lengths (Å)		1.734	1.747	1.039	1.568	1.131	1.490
Bond angles (°)		0.015	0.018	0.006	0.013	0.008	0.013

^aFor descriptions of the protein constructs, see also Table S1.

^bValues in parentheses are for the highest-resolution shell.

^cAverage over all atoms.