8OLD
Crystal structure of Archaeoglobus fulgidus AfAgo-N protein representing N-L1-L2 domains
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2) |
| Synchrotron site | PETRA III, EMBL c/o DESY |
| Beamline | P14 (MX2) |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-12-04 |
| Detector | DECTRIS PILATUS3 X 6M |
| Wavelength(s) | 0.97680 |
| Spacegroup name | P 1 |
| Unit cell lengths | 42.033, 57.843, 61.622 |
| Unit cell angles | 73.94, 89.56, 89.75 |
Refinement procedure
| Resolution | 47.630 - 1.850 |
| R-factor | 0.18299 |
| Rwork | 0.179 |
| R-free | 0.21819 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.527 |
| Data reduction software | XDS (VERSION Jun 17, 2015) |
| Data scaling software | SCALA (3.3.22 : 21/07/13) |
| Phasing software | MOLREP (Vers 9.2.10; 30.11.2005) |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 55.590 | 1.950 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.033 | |
| Rmeas | 0.044 | 0.696 |
| Rpim | 0.033 | 0.492 |
| Number of reflections | 44415 | 6503 |
| <I/σ(I)> | 15.9 | |
| Completeness [%] | 93.2 | 93.5 |
| Redundancy | 3.6 | 3.6 |
| CC(1/2) | 0.999 | 0.817 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 280 | NaCl 0.012 M; KCl 0.08 M; Sodium Cacodylate pH 6.0 0.04 M; MPD 50% ;spermin 0.012 M; 9 mg/ml protein concentration |






