Table 1

Data collection and refinement statistics


PfFeSod (PDB code 2BPI)
Data collection

X-ray source
ESRF Beamline ID29
Wavelength (Å)
0.976000
Collection Temperature (K)
100
Resolution range (Å)
25.00 – 2.52
Space group
P212121
Unit-cell parameters (Å)
a = 55.94, b = 78.91, c = 90.62
Matthews coefficient/solvent content (%)
2.2/43.0
Number of unique reflections, overall/outer shella
13247 (843)
Completeness (%), overall/outer shella
98.8 (100)
Redundancy, overall/outer shella
4.1 (4.2)
I/σ(I), overall/outer shella
17.3 (6.2)
Rmergeb (%), overall/outer shella
8.3 (29.7)


Refinement and model statistics

R-factorc
0.187 (0.224)
R-freed
0.263 (0.338)
Molecules/asymmetric unit
2
Number of protein non hydrogen atoms
3345
Number of water molecules
140
Rms deviation from targete

     Bond lengths (Å)
0.014
     Bond angles (°)
1.453
Average B-factor (Å2)
28.10
Ramachandran plotf
90.3/8.6/0.6/0.6

a Figures in parentheses concern the outer shell and corresponds to 2.582–2.520 Å.

b Rmerge = Σhkl Σi|Ii - <I> |/Σhkl Σi <I> where Ii is the intensity of the ith measurement of a reflection with indexes hkl and <I> is the statistically weighted average reflection intensity.

c R-factor = Σ ||Fo| - |Fc||/Σ |Fo| where Fo and Fc are the observed and calculated structure factor amplitudes, respectively.

d R-free is the R-factor calculated with 5 % of the reflections chosen at random and omitted from refinement.

e Root-mean-square deviation of bond lengths or bond angles from ideal geometry.

f Percentage of residues in most favoured/additionally allowed/generously allowed/disallowed regions of the Ramachandran plot, according to PROCHECK.

Boucher et al. BMC Structural Biology 2006 6:20   doi:10.1186/1472-6807-6-20