2CBY
Crystal structure of the ATP-dependent Clp Protease proteolytic subunit 1 (ClpP1) 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 | 2001-08-20 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 178.255, 178.255, 264.914 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 154.300 - 2.600 |
| R-factor | 0.194 |
| Rwork | 0.192 |
| R-free | 0.22900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tyf |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.480 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 76.700 | 2.740 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.160 | 0.690 |
| Number of reflections | 76728 | |
| <I/σ(I)> | 24.3 | 6.6 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 22.2 | 22.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | THE PROTEIN WAS CRYSTALLISED BY THE VAPOUR DIFFUSION METHOD IN HANGING DROPS CONTAINING A 1:1 MIXTURE OF 3 MG/ML PROTEIN SOLUTION (IN 50 MM TRIS-HCL PH 8) AND RESERVOIR SOLUTION INCLUDING 1 M AMMONIUM SULPHATE IN 0.1 M HEPES PH 8. |
