2GB3
Crystal structure of Aspartate aminotransferase (tm1698) from Thermotoga maritima at 2.50 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL11-1 |
| Synchrotron site | SSRL |
| Beamline | BL11-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-04-28 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 75.094, 214.051, 76.839 |
| Unit cell angles | 90.00, 112.31, 90.00 |
Refinement procedure
| Resolution | 107.030 - 2.500 |
| R-factor | 0.231 |
| Rwork | 0.229 |
| R-free | 0.26600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1xi9A |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.526 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 107.211 | 107.210 | 2.560 |
| High resolution limit [Å] | 2.496 | 11.160 | 2.500 |
| Rmerge | 0.139 | 0.057 | 0.200 |
| Total number of observations | 3894 | 9584 | |
| Number of reflections | 75747 | 888 | 5158 |
| <I/σ(I)> | 3.4 | 5.3 | 3.5 |
| Completeness [%] | 97.5 | 98.8 | 89.4 |
| Redundancy | 3.4 | 4.4 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP, NANODROP | 4.5 | 277 | 35.0% 2-propanol, 0.1M Acetate, pH 4.5, VAPOR DIFFUSION, SITTING DROP, NANODROP, temperature 277K |
