1BKG
ASPARTATE AMINOTRANSFERASE FROM THERMUS THERMOPHILUS WITH MALEATE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 287 |
Detector technology | IMAGE PLATE |
Collection date | 1997-05 |
Detector | RIGAKU |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 80.250, 109.710, 197.300 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.600 |
R-factor | 0.197 |
Rwork | 0.197 |
R-free | 0.23800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bjw |
RMSD bond length | 0.011 |
RMSD bond angle | 24.000 * |
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 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.109 | 0.335 |
Total number of observations | 185800 * | |
Number of reflections | 52952 | |
<I/σ(I)> | 5.9 | 1.06 |
Completeness [%] | 97.3 | 89.9 |
Redundancy | 3.6 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7 * | 20 * | pH 6.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | drop | maleate | 40 (mM) | |
3 | 1 | drop | 100 (mM) | ||
4 | 1 | drop | HEPES | 2 (mM) | |
5 | 1 | reservoir | sodium acetate | 200 (mM) | |
6 | 1 | reservoir | sodium citrate | 100 (mM) | |
7 | 1 | reservoir | PEG6000 | 16 (%) |