3H0R
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 | 2007-03-20 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 1 |
| Unit cell lengths | 127.377, 130.411, 153.973 |
| Unit cell angles | 89.89, 90.21, 89.95 |
Refinement procedure
| Resolution | 48.970 - 3.000 |
| R-factor | 0.26515 |
| Rwork | 0.263 |
| R-free | 0.30604 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3h0l |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.482 |
| 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] | 49.000 | 3.110 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.112 | 0.710 |
| Number of reflections | 182013 | |
| <I/σ(I)> | 5.8 | 1.2 |
| Completeness [%] | 91.2 | 84.5 |
| Redundancy | 1.7 | 1.6 |
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 Asn, 0.6mM ATP) mix with well solution (10-12% PEG3350, 10mM Mg formate), crystal soaked in the mother liquor with 10mMAsn, 10mM Asp, 10mM ATP, 10mM MnCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
