1DZF
RPB5 from S.cerevisiae
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.6 |
Synchrotron site | SRS |
Beamline | PX9.6 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-05-15 |
Detector | ADSC QUANTUM 4 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 45.050, 82.220, 134.810 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.900 |
R-factor | 0.217 |
Rwork | 0.217 |
R-free | 0.27100 |
Structure solution method | MAD |
RMSD bond length | 0.009 |
RMSD bond angle | 25.300 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 |
Phasing software | X-PLOR (3.8) |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.054 * | 0.226 * |
Number of reflections | 19245 | |
<I/σ(I)> | 8.1 | 2.9 |
Completeness [%] | 96.9 | 98.2 |
Redundancy | 4.7 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | 4 * | PROTEIN WAS CRYSTALLIZED FROM 20% PEG 800, 200 MM AMMONIUM SA SULPHATE, 100 MM SODIUM CACODYLATE, PH 6.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15-20 (mg/ml) | |
2 | 1 | reservoir | PEG8000 | 20-24 (%) | |
3 | 1 | reservoir | glycerol | 15 (%) | |
4 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
5 | 1 | reservoir | sodium cacodylate | 0.1 (M) |