Tabel I.
Summary of Data Collection and Refinement Statistics of the FYR Domain of TBRG1
| Native | SeMet | |||
|---|---|---|---|---|
| Data collection | ||||
| Space group | P3121 | P3121 | ||
| Cell dimensions | ||||
| a, b, c (Å) | 53.867, 53.867, 91.297 | 53.976, 53.976, 91.297 | ||
| α, β, γ (°) | 90, 90, 120 | 90, 90, 120 | ||
| Molecules/AU | 1 | 1 | ||
| Peak | Inflection | Remote | ||
| Wavelength (Å) | 0.9796 | 0.9797 | 0.9798 | 0.9763 |
| Resolution (Å) | 32.6–1.6 | 41.6–2.0 | 32.6–2.0 | 32.6–2.0 |
| Rsym or Rmergea | 0.079 (0.422) | 0.068 (0.163) | 0.054 (0.134) | 0.059 (0.160) |
| I/σI | 18.8 (5.7) | 23.7 (12.3) | 20.0 (10.0) | 17.4 (8.3) |
| Completeness (%) | 99.8 (98.9) | 98.7 (97.9) | 98.9 (98.0) | 98.5 (97.6) |
| Redundancy | 10.3 (10.4) | 10.5 (10.9) | 5.3 (5.5) | 5.3 (5.5) |
| Refinement | ||||
| Resolution (Å) | 23.3–1.6 | |||
| No. reflections | 20876 | |||
| Rworkb/Rfreec | 0.178, 0.202 | |||
| No. atoms | ||||
| Protein | 1118 | |||
| Ligand/ion | 6 (2 Glycerol) | |||
| Water | 160 | |||
| B-factors (Å2) | ||||
| Protein | 19.64 | |||
| Ligand/ion | 28.09 | |||
| Water | 29.24 | |||
| R.M.S.D.d | ||||
| Bond lengths (Å) | 0.012 | |||
| Bond angles (°) | 1.391 | |||
| Ramachandrane | 90.0%, 0.0% | |||
Values in parentheses refer to the last resolution shell.
a
Rsym = ΣhΣi|I(h,i)−I(h)|/ΣhΣi I(h,i) where I(h,i) are symmetry related intensities and I(h) is the mean intensity of the reflection with unique index h.
b
Rcryst (%) = Σ|Fo − Fc|/ΣFo, where, Fo is the observed structure factor amplitude, and Fc is the structure factor calculated from the model.
c
Rfree (%) is calculated in the same manner as Rcryst using 5% of all reflections excluded from refinement stages using high-resolution data.
d
R.M.S.D., root-mean-square deviation.
e
Percentage of residues in the “most favored region” of the Ramachandran plot and percentage of outliers (PROCHECK).