1H0C
The crystal structure of human alanine:glyoxylate aminotransferase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2002-01-15 |
Detector | ADSC CCD |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 90.330, 90.330, 142.010 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 * - 2.500 |
R-factor | 0.231 |
Rwork | 0.231 |
R-free | 0.28600 |
Structure solution method | OTHER |
RMSD bond length | 0.014 |
RMSD bond angle | 1.700 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE/RESOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.580 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.074 | 0.177 |
Total number of observations | 161988 * | |
Number of reflections | 21044 | |
<I/σ(I)> | 6.9 | 3.8 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 7.7 | 7.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 7.5 | 293 * | Zhang, X., (2001) Acta Crystallogr., D57, 1936. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 15 (mg/ml) | |
2 | 1 | 1 | PEG4000 | 10 (%) | |
3 | 1 | 1 | sodium HEPES | 0.1 (M) | pH7.5 |