1HJ9
Atomic resolution structures of trypsin provide insight into structural radiation damage
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM1A |
Synchrotron site | ESRF |
Beamline | BM1A |
Temperature [K] | 120 |
Detector technology | IMAGE PLATE |
Collection date | 2000-06-15 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 54.055, 56.812, 66.282 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 0.950 |
R-factor | 0.1171 |
R-free | 0.13990 |
Structure solution method | OTHER |
RMSD bond length | 0.018 |
RMSD bond angle | 0.035 |
Data reduction software | DENZO |
Data scaling software | SCALA |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.000 |
High resolution limit [Å] | 0.950 | 0.950 |
Rmerge | 0.048 | 0.472 |
Total number of observations | 886215 * | |
Number of reflections | 128074 | |
<I/σ(I)> | 7.3 | 1.6 |
Completeness [%] | 99.5 | 99.6 * |
Redundancy | 6.9 | 5.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8 | pH 8.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG8000 | 25 (%) | |
2 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
3 | 1 | reservoir | Tris | 0.1 (M) | pH8. |
4 | 1 | reservoir | aniline | 0.1 (M) | |
5 | 1 | drop | protein | 15 (mg/ml) |