3IGR
The Crystal Structure of Ribosomal-protein-S5-alanine Acetyltransferase from Vibrio fischeri to 2.0A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-06-19 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9794 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 63.504, 107.173, 145.719 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.207 |
Rwork | 0.205 |
R-free | 0.23700 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.278 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC (refmac_5.5.0102) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 4.310 | 2.000 |
Rmerge | 0.094 | 0.056 | 0.700 |
Number of reflections | 34070 | ||
<I/σ(I)> | 6.4 | ||
Completeness [%] | 99.8 | 98.9 | 100 |
Redundancy | 4.9 | 4.8 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 9 | 277 | 10% PEG 20000, 2% Dioxane, 0.1M Bicine pH 9, VAPOR DIFFUSION, SITTING DROP, temperature 277K |