BMC Structural Biology

Table 1 X-Ray Data Processing and Refinement Statistics

From: Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal site

	ybgI native	ybgI SeMet
diffraction data
space group	P3	P3
cell (a,b,c) (Å)	156.7,156.7,57.6	154.7,154.7,57.5
resolution (Å)	2.2	2.2
wavelength (Å)	0.9795	0.9793	0.9795	0.9780
no. measured intensities	303,926	298,729	298,987	297,849
no. unique reflection	80,094	77,951	77,981	77,584
mean redundancy	5	2	2	2
R merge (all/high res.)	0.096/0.237	0.056/0.199	0.060/0.216	0.053/0.190
completeness (all/high res.)	99.8/99.6	97.7/86.7	97.6/86.3	97.8/88.8
I/s average (all/high res.)	14.1/2.8	24.3/3.8	23.7/3.5	25.6/4.2
Refinement
resolution limits used (Å)	20.0-2.2	20.0-2.2
R-factor (95% data)	0.213	0.213
R_free (5% data)	0.252	0.260
amino acid residues/atoms	1482/11382	1482/11382
non-protein atoms	11 Mg ions	12 Fe ions
no. of water molecules	576	637
bond length rms deviation (Å)	0.026	0.025
angle rms deviation (°)	2.2	2.4
average B (main/side chain) (Å²)	15.3/16.5	18.3/19.1
average B water (Å²)	20.4	24.4

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