1GC3
THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2 COMPLEXED WITH TRYPTOPHAN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1999-09-24 |
Detector | RIGAKU RAXIS |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 81.500, 98.400, 187.000 |
Unit cell angles | 90.00, 91.53, 90.00 |
Refinement procedure
Resolution | 8.000 - 3.300 |
R-factor | 0.203 * |
Rwork | 0.203 |
R-free | 0.28200 |
RMSD bond length | 0.011 |
RMSD bond angle | 2.471 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.420 |
High resolution limit [Å] | 3.300 | 3.300 |
Rmerge | 0.099 | 0.204 |
Total number of observations | 107884 * | |
Number of reflections | 42535 | |
<I/σ(I)> | 4.9 | |
Completeness [%] | 96.0 | 92.8 |
Redundancy | 2.5 | 9.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 * | 293 | PEG 6000, HEPES, sodium acetate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
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) | |
3 | 1 | drop | 10 (mM) | ||
4 | 1 | reservoir | PEG6000 | 24 (%(w/w)) | |
5 | 1 | reservoir | HEPES | 100 (mM) |