5DLL
Aminopeptidase N (pepN) from Francisella tularensis subsp. tularensis SCHU S4
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-04 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 31 |
| Unit cell lengths | 75.670, 75.670, 161.042 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 65.530 - 2.510 |
| R-factor | 0.19653 |
| Rwork | 0.193 |
| R-free | 0.25998 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2dq6 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.931 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 65.530 | 2.520 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.104 | 0.000 |
| Number of reflections | 26293 | |
| <I/σ(I)> | 15.2 | 0.921 |
| Completeness [%] | 99.9 | 99.8 |
| Redundancy | 5.4 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.2 M Sodium iodide 0.1 M Bis Tris propane pH 6.5 20% (w/v) PEG |
