5UQ4
Crystal structure of Heme-Degrading Protein Rv3592 from Mycobacterium tuberculosis - heme free with cleaved protein
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 | 2011-10-06 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97924 |
| Spacegroup name | P 61 |
| Unit cell lengths | 38.134, 38.134, 238.638 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 33.025 - 2.201 |
| R-factor | 0.1761 |
| Rwork | 0.172 |
| R-free | 0.22310 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3hx9 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.469 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | PHENIX (dev_2650) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 5.970 | 2.200 |
| Rmerge | 0.099 | 0.043 | 1.099 |
| Rmeas | 0.104 | 0.045 | 1.196 |
| Rpim | 0.032 | 0.014 | 0.460 |
| Total number of observations | 101734 | ||
| Number of reflections | 10093 | ||
| <I/σ(I)> | 9.8 | ||
| Completeness [%] | 99.9 | 99.1 | 100 |
| Redundancy | 10.1 | 10.8 | 5.4 |
| CC(1/2) | 0.997 | 0.772 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 277 | 0.2M magnesium chloride, 0.1M bi-Tris, 25% PEG3350 |
