1R6C
High resolution structure of ClpN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X9B |
Synchrotron site | NSLS |
Beamline | X9B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2000-06-15 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.98 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 36.040, 51.990, 65.133 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.150 |
Rwork | 0.167 |
R-free | 0.24326 |
Structure solution method | MIR |
RMSD bond length | 0.024 |
RMSD bond angle | 0.759 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.230 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.026 | 0.052 |
Number of reflections | 6243 | |
<I/σ(I)> | 51.1 | 27.48 |
Completeness [%] | 0.9 | 0.744 |
Redundancy | 5.5 | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | HANGING DROP | 294 | 0.02M HEPES at pH 7.4 (protein solution) mixed 1:1 with 0.1M PIPES at pH 7.0, 35% (w/v) PEG 8000, 0.32M sodium citrate, HANGING DROP, temperature 294K |