1XFO
Crystal Structure of an archaeal aminopeptidase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-04-11 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.933 |
| Spacegroup name | P 63 |
| Unit cell lengths | 158.340, 158.340, 114.460 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 29.920 - 1.960 |
| R-factor | 0.18341 |
| Rwork | 0.183 |
| R-free | 0.20930 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vhe |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.316 |
| Data reduction software | MOSFLM |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.070 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.037 | 0.193 |
| Number of reflections | 110425 | |
| <I/σ(I)> | 24.3 | 5.2 |
| Completeness [%] | 100.0 | 63.5 |
| Redundancy | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 293 | PEG 400, sodium chloride, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
