1ZJC
Aminopeptidase S from S. aureus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
| Synchrotron site | MPG/DESY, HAMBURG |
| Beamline | BW6 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-04-28 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.05 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 70.181, 81.858, 152.885 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.800 |
| R-factor | 0.17202 |
| Rwork | 0.170 |
| R-free | 0.21154 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | authors' current unpublished structure of a thermophilic homologue of AmpS |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.756 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.064 | 0.396 |
| Number of reflections | 40684 | |
| <I/σ(I)> | 26 | 2.3 |
| Completeness [%] | 98.2 | 96.9 |
| Redundancy | 5 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 292 | HEPES/NaOH, ammonium sulfate, PEG 6K, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 292K |
