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 shell^a

13247 (843)

Completeness (%), overall/outer shell^a

98.8 (100)

Redundancy, overall/outer shell^a

4.1 (4.2)

I/σ(I), overall/outer shell^a

17.3 (6.2)

R_merge^b (%), overall/outer shell^a

8.3 (29.7)

Refinement and model statistics

R-factor^c

0.187 (0.224)

R-free^d

0.263 (0.338)

Molecules/asymmetric unit

2

Number of protein non hydrogen atoms

3345

Number of water molecules

140

Rms deviation from target^e

Bond lengths (Å)

0.014

Bond angles (°)

1.453

Average B-factor (Ų)

28.10

Ramachandran plot^f

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 R_merge = Σ_hkl Σ_i|I_i - <I> |/Σ_hkl Σ_i <I> where I_i 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 ||F_o| - |F_c||/Σ |F_o| where F_o and F_c 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