5DS0
Crystal structure of TET aminopeptidase from marine sediment archaeon Thaumarchaeota archaeon SCGC AB-539-E09
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 | 2014-08-24 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97915 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 114.638, 165.372, 125.789 |
| Unit cell angles | 90.00, 90.87, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.800 |
| R-factor | 0.19308 |
| Rwork | 0.193 |
| R-free | 0.20612 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1vhe |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.369 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.850 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.161 | 0.800 |
| Number of reflections | 116464 | |
| <I/σ(I)> | 10.81 | 1.85 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 277 | 0.1 M magnesium formate, 15% PEG3350, 2.6 mM CoCl2, 2.6 mM L-Phe-AMC, cryo 25% glycerol |
