1BJW
ASPARTATE AMINOTRANSFERASE FROM THERMUS THERMOPHILUS
Experimental procedure
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 |
Detector | RIGAKU |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 61.600, 113.860, 124.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.800 |
R-factor | 0.215 |
Rwork | 0.215 |
R-free | 0.26900 |
Structure solution method | ISOMORPHOUS REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 24.200 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.851) |
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 | 0.075 | 0.235 |
Total number of observations | 149097 * | |
Number of reflections | 74202 | |
<I/σ(I)> | 15 | 2.8 |
Completeness [%] | 90.7 | 0.235 |
Redundancy | 2.2 | 1.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 * | 293 * | Nakai, T., (1998) Acta Crystallogr. D54, 1032. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | 100 (mM) | ||
3 | 1 | drop | HEPES | 2 (mM) | |
4 | 1 | reservoir | ammonium phosphate | 300 (mM) |