5XPG
Crystal structure of T. thermophilus Argonaute protein complexed with a bulge 6'U7' on the target strand
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-03-15 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97926 |
| Spacegroup name | P 41 3 2 |
| Unit cell lengths | 202.351, 202.351, 202.351 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 49.080 - 2.800 |
| R-factor | 0.205 |
| Rwork | 0.203 |
| R-free | 0.24600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3dlh |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.201 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (PHENIX.REFINE) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.086 | 0.389 |
| Number of reflections | 35223 | |
| <I/σ(I)> | 21.6 | 2.2 |
| Completeness [%] | 99.5 | 98.3 |
| Redundancy | 8.7 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 308 | 1.0 M (NH4)2SO4, 0.1 M KCL, 10 MM MGCL2, 50 MM BIS-TRIS PH 6.5 , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 308K |






