4PF1
Crystal structure of aminopeptidase from marine sediment archaeon Thaumarchaeota archaeon
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-10-16 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.979268 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 118.434, 108.144, 120.384 |
| Unit cell angles | 90.00, 95.08, 90.00 |
Refinement procedure
| Resolution | 29.690 - 2.100 |
| R-factor | 0.2054 |
| Rwork | 0.205 |
| R-free | 0.22880 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mpx |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.730 |
| Data scaling software | HKL-3000 |
| Phasing software | MOLREP |
| Refinement software | BUSTER (2.10.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.140 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.137 | 0.570 |
| Number of reflections | 176530 | |
| <I/σ(I)> | 9 | |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 3.2 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 277 | 0.2 M Na citrate, 20% PEG3350, 2.8 mM DL-Phe |
