3S0Q
Peptidase module of the peptidoglycan hydrolase RipA (Rv1477) from Mycobacterium tuberculosis, catalytic site mutant (Cys383Ala) at 1.45 resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-2 |
| Synchrotron site | MAX II |
| Beamline | I911-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-01 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 1.03873 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 36.830, 65.850, 68.010 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 18.570 - 1.450 |
| R-factor | 0.15296 |
| Rwork | 0.152 |
| R-free | 0.17827 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.498 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 18.670 | 1.530 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.068 | 0.375 |
| Number of reflections | 29973 | |
| <I/σ(I)> | 15.1 | 4 |
| Completeness [%] | 99.1 | 94.4 |
| Redundancy | 4.8 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 35% PEG400, 0.2M LiSO4, Tris-HCl pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
