3BQO
Crystal Structure of TRF1 TRFH domain and TIN2 peptide complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-D |
Synchrotron site | APS |
Beamline | 23-ID-D |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-07-19 |
Detector | MARMOSAIC 300 mm CCD |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 117.105, 117.105, 88.018 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
Rwork | 0.220 |
R-free | 0.23690 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1h6o |
RMSD bond length | 0.006 |
RMSD bond angle | 1.237 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.074 | 0.443 |
Number of reflections | 24517 | |
<I/σ(I)> | 50.3 | 7.4 |
Completeness [%] | 99.9 | 100 |
Redundancy | 20.2 | 18.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.6 | 289 | NaCl 2.5 M MgCl2 0.35 M Tris 0.1 M pH 8.6 DTT 5 mM , VAPOR DIFFUSION, HANGING DROP, temperature 289K |