1B5P
THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-6A |
| Synchrotron site | Photon Factory |
| Beamline | BL-6A |
| Temperature [K] | 287 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-02-15 |
| Detector | RIGAKU |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 61.490, 113.620, 124.400 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.800 |
| R-factor | 0.193 |
| Rwork | 0.193 |
| R-free | 0.23900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1bjw |
| RMSD bond length | 0.010 |
| RMSD bond angle | 24.400 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.066 | 0.248 |
| Total number of observations | 169852 * | |
| Number of reflections | 73849 | |
| <I/σ(I)> | 15 | 2.1 |
| Completeness [%] | 90.6 | 83.8 |
| Redundancy | 2.3 | 1.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 * | CRYSTALLIZED FROM 300MM AMMONIUM PHOSPHATE, PH 4.3 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 0.2 (mM) | |
| 2 | 1 | drop | HEPES | 5 (mM) | pH8.0 |
| 3 | 1 | drop | 10 (mM) | ||
| 4 | 1 | reservoir | PEG6000 | 16 (%(w/w)) | |
| 5 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |
