Table 1 Crystallographic data and refinement statistics.

From: The Arabidopsis glutamyl-tRNA reductase (GluTR) forms a ternary complex with FLU and GluTR-binding protein

PDB code

5CHE

Data collection

 Space group

C2

 Unit cell dimensions

  a, b, c (Å)

217.0, 53.2, 203.8

  α, β, γ (°)

90.0, 108.4, 90.0

 Wavelength (Å)

0.9793

 Resolution (Å)

50.0–3.20 (3.31–3.20)

 No. of measured reflections

156901

 No. of unique reflections

36775 (3661)

 Completeness (%)

99.6 (99.9)

 Redundancy

4.3 (4.3)

 I/σI

10.0 (1.7)

 Rmerge

0.132 (0.831)

Refinement statistics

 Resolution (Å)

39.27–3.20 (3.30–3.20)

 Rwork/Rfree(%)

22.3/27.8

 Number of atoms

  Protein

12365

  Water

6

 Average B value (Å2)

25.78

 R.m.s deviations

 

  Bond lengths (Å)

0.006

  Bond angles (°)

0.975

 Ramachandran plot

 

  Most favored (%)

96.67

  Additional allowed (%)

3.01

  Disallowed (%)

0.32

  1. Rmerge = ΣhklΣi|Ihkl,i − Im|/ΣhklΣiIhkl,i, where Ihkl,i is the intensity of the measured reflection and Im is the mean intensity of the symmetry-related reflections after rejections. R = Σ||Fo| − |Fc||/Σ|Fo|, where Fo and Fc are the observed and calculated structure factors, respectively. Rfree is the cross-validated R-factor computed for a test set of 5% of the reflections, which were omitted during refinement. The values in parentheses relate to the highest resolution shell.
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