1GVX
Endothiapepsin complexed with H256
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 130 |
| Detector technology | CCD |
| Collection date | 2001-04-01 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.881, 75.446, 43.226 |
| Unit cell angles | 90.00, 97.47, 90.00 |
Refinement procedure
| Resolution | 10.000 - 1.000 |
| R-factor | 0.14 |
| R-free | 0.16470 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3er5 |
| RMSD bond length | 0.026 |
| RMSD bond angle | 0.048 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 10.000 | 1.050 |
| High resolution limit [Å] | 1.000 | 1.000 |
| Rmerge | 0.079 | 0.163 |
| Number of reflections | 136765 | |
| <I/σ(I)> | 12.7 | 3.6 |
| Completeness [%] | 96.9 | 94.3 |
| Redundancy | 6.9 | 6.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 4.5 | PH 4.50 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | enzyme | 2.0 (mg/ml) | |
| 2 | 1 | 1 | sodium acetate | 100 (mM) |
