Table 1

X-ray data collection (ESRF) and refinement statistics

Data collection
TPK Thiamine-PNP
TPK Thiamine

Beam line
ID29
BM30A
Wavelength (Å)
0.98
0.954
Space group
P1
P1
Unit cell (Å)
a = 50.825 b = 60.331 c = 63.722
a = 51.309 b = 60.696 c = 64.831
100 K
α = 66.144 β = 89.941 γ = 65.067
α = 65.937 β = 89.858 γ = 64.868
Resolution range (Å)(highest resolution shell)
29.45 to 1.96(2.03 to 1.96)
50.19 to 2.1(2.21 to 2.1)
Observations
70690 (104)
68171 (8700)
Unique reflections
35345 (52)
33349 (4258)
Multiplicity1
1.9 (1.0)
2 (2)
Completeness1
92.8 (60.3)
96.1 (85.4)
<I/σI>1,2
14.5 (3.8)
7.9 (7.1)
Rsym (%)1,3
3.5 (19.5)
4.7 (8.3)

Refinement
2G9Z
2HH9

Rcryst (%)4
18.7 (31)
18.1 (21)
Rfree (%)
23.6 (33)
25.4 (26)
Δbond (Å)
0.022
0.05
Δangle (°)
1.934
1.2
N° Protein atoms
4776
4786
N° water
520
660
N° Heterogen atoms
62
40
Average B factor (Å2)
26.9
26.2
     Protein main chain
26
25.9
     Water
41
45.8
     Ligand
18.1
20.4
     Mg2+
23.58
8.4
     PO4
31.6

     Cl-
29.8

Ramachandran plot (%)


     Most favored
79.2
76.0
     Allowed
9.0
11.8
     Generously allowed
0.3
0.3
     Disallowed regions
0.3
0.3

1 values in parentheses are for the highest resolution shell.

2 < I/σI>, is the mean signal to noise ratio, where I is the integrated intensity of a measured reflection and σ is the estimated error in the measurement.

3 Rsym = ∑h i|Ih, i - ⟨Ih⟩|/∑h i|Ih, i, where I is the integrated intensity of reflection h having i observations and ⟨Ih⟩ is the mean recorded intensity of reflection h over multiple recording.

4 Rcryst = ∑||Fo|-|Fc||/∑|Fo|, where Fo are observed and Fc calculated structure factor amplitudes. Rfree is calculated from a randomly chosen 9.9% of reflections.

Santini et al. BMC Structural Biology 2008 8:33   doi:10.1186/1472-6807-8-33