3ROR
Crystal structure of C105S mutant of Mycobacterium tuberculosis methionine aminopeptidase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-07-09 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.220, 48.660, 55.720 |
| Unit cell angles | 90.00, 95.16, 90.00 |
Refinement procedure
| Resolution | 28.520 - 2.000 |
| R-factor | 0.2142 |
| Rwork | 0.211 |
| R-free | 0.27370 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1y1n |
| RMSD bond length | 0.021 |
| RMSD bond angle | 1.924 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.500 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.154 | 0.399 |
| Number of reflections | 15726 | |
| <I/σ(I)> | 5.6 | 2.1 |
| Completeness [%] | 87.8 | 90.8 |
| Redundancy | 2.8 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 298 | PEG 2000, Bistris, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
