. 2011 Mar 18;6(3):e17624. doi: 10.1371/journal.pone.0017624

Table 1. Summary of crystal parameters, data collection and refinement statistics for PDB 3hn7.

Space group	C2
Unit cell parameters	a = 105.45 Å, b = 52.76 Å, c = 89.99 Å, β = 98.47°
Data collection	λ₁ MAD-Se	λ₂ MAD-Se	λ₃ MAD-Se
Wavelength (Å)	0.9116	0.9793	0.9792
Resolution range (Å)	29.0–1.65	29.0–1.65	29.0–1.69
Number of observations	196,918	195,361	182,672
Number of unique reflections	59,026	58,985	55,004
Completeness (%)	100 (100)^a	100 (100)^a	100 (100)^a
Mean I/σ(I)	11.5 (2.2)^a	9.9 (1.7)^a	10.5 (1.8)^a
Rsym on I (%)	0.076 (0.51)^a	0.093 (0.58)^a	0.085 (0.54)^a
Highest resolution shell (Å)	1.69–1.65	1.69–1.65	1.73–1.69
Model and refinement statistics
Resolution range (Å)	29.0–1.65	Data set used in refinement	λ₁ MAD-Se
No. of reflections (total)	59,024^b	Cutoff criteria	\|F\|>0
No. of reflections (test)	2,985	R_cryst	0.154
Completeness (% total)	100	R_free	0.187
Stereochemical parameters
Restraints (RMSD observed)
Bond angle (°)	1.59
Bond length (Å)	0.018
Average protein isotropic B-value (Å²)	19.6^c
ESU based on R_free (Å)	0.087
No. of protein residues/atoms	480/3728
No. of water molecules	588 (with 10 modeled in alternate positions)

Highest resolution shell.

ESU = Estimated overall coordinate error [33].

R_sym = Σ|I_i-<I_i>|/Σ|I_i|, where I_i is the scaled intensity of the i^th measurement and <I_i> is the mean intensity for that reflection.

R_cryst = Σ||F_obs|-|F_calc||/Σ|F_obs|, where F_calc and F_obs are the calculated and observed structure factor amplitudes, respectively.

R_free = as for R_cryst, but for 5.1% of the total reflections chosen at random and omitted from refinement.

Typically, the number of unique reflections used in refinement is slightly less that the total number that were integrated and scaled. Reflections are excluded due to negative intensities and rounding errors in the resolution limits and cell parameters.

This value represents the total B that includes TLS and residual B components.