3P32
Hydrolysis of GTP to GDP by an MCM-associated and MeaB- and MMAA-like G-protein from Mycobacterium tuberculosis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-05-21 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97946 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 65.860, 188.220, 66.500 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.427 - 1.900 |
| R-factor | 0.1998 |
| Rwork | 0.199 |
| R-free | 0.22260 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3mdo |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.406 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.950 | |
| High resolution limit [Å] | 1.900 | 8.500 | 1.900 |
| Rmerge | 0.044 | 0.017 | 0.555 |
| Number of reflections | 32985 | 407 | 2409 |
| <I/σ(I)> | 25.16 | 63.3 | 3.5 |
| Completeness [%] | 99.8 | 94.7 | 99.4 |
| Redundancy | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.2 | 289 | 22.0 mg/mL MytuD00200aA1 PW25862 against 48% PEG 200, 0.1 M Na/K phosphate pH 6.2, 0.2 M NaCl, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
