4ICR
Structural basis for substrate recognition and reaction mechanism of bacterial aminopeptidase peps
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PAL/PLS BEAMLINE 6B |
| Synchrotron site | PAL/PLS |
| Beamline | 6B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | BRUKER PROTEUM 300 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 94.278, 185.277, 59.237 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.320 - 2.170 |
| R-factor | 0.232 |
| Rwork | 0.229 |
| R-free | 0.30000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.025 |
| RMSD bond angle | 1.927 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | EPMR |
| Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.230 |
| High resolution limit [Å] | 2.170 | 2.170 |
| Number of reflections | 55718 | |
| <I/σ(I)> | 19.97 | 8 |
| Completeness [%] | 99.6 | 100 |
| Redundancy | 7.2 | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 10% 2-PROPANOL, 0.2M ZINC ACETATE, PH 6.5, MICROBATCH, TEMPERATURE 295K |
