3H0M
Structure of trna-dependent amidotransferase gatcab from aquifex aeolicus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-12-19 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0274 |
| Spacegroup name | P 1 |
| Unit cell lengths | 128.248, 129.856, 155.069 |
| Unit cell angles | 90.01, 89.96, 90.11 |
Refinement procedure
| Resolution | 39.370 - 2.800 |
| R-factor | 0.25623 |
| Rwork | 0.254 |
| R-free | 0.30540 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2h0l |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.491 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASES |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.400 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.061 | 0.478 |
| Number of reflections | 241473 | |
| <I/σ(I)> | 11.5 | 1.6 |
| Completeness [%] | 98.0 | 96.8 |
| Redundancy | 2 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 1:1 ratio of Protein solution (6-9mg/ml GatCAB,10mM HEPES, 50uM Zn acetate,10mM Gln, 0.6mM ATP) mix with well solution (10-12% PEG3350, 10mM Mg formate), pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
