1G12
ZINC PEPTIDASE FROM GRIFOLA FRONDOSA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL45XU |
| Synchrotron site | SPring-8 |
| Beamline | BL45XU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-02-11 |
| Detector | RIGAKU RAXIS IV |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 43.631, 41.757, 76.941 |
| Unit cell angles | 90.00, 95.48, 90.00 |
Refinement procedure
| Resolution | 38.300 - 1.600 |
| Rwork | 0.218 |
| R-free | 0.22900 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.060 |
| Data reduction software | PROCESS |
| Data scaling software | PROCESS ((RIGAKU)) |
| Phasing software | DM |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 38.300 | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.069 | 0.195 |
| Total number of observations | 96644 * | |
| Number of reflections | 15467 * | |
| <I/σ(I)> | 21.4 | |
| Completeness [%] | 84.3 | 40.9 |
| Redundancy | 6.3 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 * | 293 * | drop consists of equal amounts of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | acetate | 10 (mM) | |
| 3 | 1 | reservoir | 0.1-3.0 (M) | ||
| 4 | 1 | reservoir | imidazole | 10 (mM) |
