1I6V
THERMUS AQUATICUS CORE RNA POLYMERASE-RIFAMPICIN COMPLEX
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 | 1999-09-10 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.03321 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 199.450, 199.450, 289.130 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 3.300 |
R-factor | 0.28 |
Rwork | 0.276 |
R-free | 0.35900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1DDQ |
RMSD bond length | 0.009 |
RMSD bond angle | 1.750 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.420 |
High resolution limit [Å] | 3.300 | 3.300 |
Rmerge | 0.077 | 0.344 |
Total number of observations | 214453 * | |
Number of reflections | 75420 | 6173 * |
<I/σ(I)> | 10.67 | 1.67 |
Completeness [%] | 86.1 | 71.7 |
Redundancy | 2.8 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | drop consists of equal amounts of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 17 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 40-45 (%sat) | |
3 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
4 | 1 | reservoir | 20 (mM) |