3BUA
Crystal Structure of TRF2 TRFH domain and APOLLO peptide complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Detector technology | CCD |
Collection date | 2007-02-08 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.97869 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 109.947, 109.947, 130.830 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.500 |
Rwork | 0.229 |
R-free | 0.25440 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1h6p |
RMSD bond length | 0.006 |
RMSD bond angle | 1.628 |
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 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.086 | 0.610 |
Number of reflections | 31885 | |
<I/σ(I)> | 30 | 2.51 |
Completeness [%] | 99.9 | 99.2 |
Redundancy | 10.8 | 8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 289 | (NH4)2SO4 2.6 M DTT 1 mM MES 0.05 M pH 5.6 MgAc2 10 mM, VAPOR DIFFUSION, HANGING DROP, temperature 289K |