2C8T
The 3.0 A Resolution Structure of Caseinolytic Clp Protease 1 from Mycobacterium tuberculosis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Collection date | 2005-03-07 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 96.719, 168.218, 103.761 |
| Unit cell angles | 90.00, 114.60, 90.00 |
Refinement procedure
| Resolution | 19.870 - 3.000 |
| R-factor | 0.214 |
| Rwork | 0.213 |
| R-free | 0.23800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tyf |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.447 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 59.400 | 3.160 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.100 | 0.400 |
| Number of reflections | 60193 | |
| <I/σ(I)> | 5.9 | |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.2 | 5 MG/ML PROTEIN, 100 MM TRI-NA-CITRATE, PH 5.2, 3% PEG 4000 |
