1GCK
THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1 COMPLEXED WITH ASPARTATE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1999-08-25 |
Detector | RIGAKU RAXIS |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 62.750, 74.890, 163.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.500 |
R-factor | 0.217 |
Rwork | 0.205 |
R-free | 0.28400 |
RMSD bond length | 0.014 |
RMSD bond angle | 2.000 * |
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 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.067 | 0.218 |
Total number of observations | 82422 * | |
Number of reflections | 24644 | |
<I/σ(I)> | 9.4 | |
Completeness [%] | 89.5 | 88.7 |
Redundancy | 3.3 | 9.6 |
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) | pH8.0 |
3 | 1 | drop | 10 (mM) | ||
4 | 1 | reservoir | PEG6000 | 24 (%(w/w)) | |
5 | 1 | reservoir | HEPES | 100 (mM) |