3BWO
L-tryptophan aminotransferase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL1-5 |
| Synchrotron site | SSRL |
| Beamline | BL1-5 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97944 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 93.330, 98.660, 139.360 |
| Unit cell angles | 90.00, 104.50, 90.00 |
Refinement procedure
| Resolution | 29.660 - 2.400 |
| R-factor | 0.23844 |
| Rwork | 0.238 |
| R-free | 0.25272 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1lk9 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.596 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.460 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Number of reflections | 91359 | |
| <I/σ(I)> | 11.69 | 3.39 |
| Completeness [%] | 95.3 | 91.3 |
| Redundancy | 3.81 | 3.87 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | 13-19% PEG 3350, 0.3M KCl, 100mM MOPSO pH7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
