TABLE 1.

X-ray data collection and refinement statistics

The highest resolution shell values are shown in parentheses.

Data set	Tetrasulfide dimer	Tetrasulfide dimer reduced	Nonasulfide dimer	Bet v 1 Y5F
Accession number	4BKC	4BK6	4BKD	4BK7
Data collection
Space group	P21	P21	C2	P21
Cell dimensions
a, b, c (Å)	39.9, 61.0, 59.7	40.1, 61.2 60.1	112.9, 44.7, 32.0	32.7, 55.8, 38.1
α, β, γ	90, 107, 90	90, 107, 90	90, 91, 90	90, 93, 90
Wavelength (Å)	0.8865	0.8865	0.8865	0.8865
Number of unique reflections	27,922	34,452	52,883	47,976
Resolution (Å)	41.62-1.73	57.33-1.63	56.45-1.17	55.81-1.14
Rmerge (%)	0.119 (0.634)	0.062 (0.615)	0.027 (0.594)	0.035 (0.268)
Completeness (%)	98.1 (98.0)	99.5 (99.0)	97.8 (91.4)	96.3 (80.7)
Redundancy	3.0 (3.0)	3.4 (3.5)	3.2 (2.8)	3.2 (2.4)
I/σ(I)	5.7 (1.1)	13.2 (1.9)	17.0 (2.0)	17.1 (3.5)
Wilson B-factor	19.5	20.6	13.5	9.4
Refinement statistics
Resolution range (Å)	56.97–1.73	57.33–1.63	56.45–1.17	38.04–1.14
Number of unique reflections	26,644	32,699	50,194	45,515
Rwork/Rfree (%)	20.12/24.67	18.1/23.8	17.7/20.2	13.4/17.5
Number of atoms
Protein	2,533	2,548	1,319	1,403
Water	219	428	198	209
RMSD from ideal values
Bond lengths (Å)	0.005	0.004	0.008	0.012
Bond angles (°)	0.906	0.930	1.431	1.547
Average B-factors (Å2)
Protein	19.56	19.54	17.07	12.47
Solvent	24.60	29.94	27.59	25.94