1W0T
hTRF1 DNA-binding domain in complex with telomeric DNA.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-11-15 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 38.443, 72.360, 116.706 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 23.620 - 2.000 |
R-factor | 0.252 |
Rwork | 0.252 |
R-free | 0.27300 |
Structure solution method | MIR |
RMSD bond length | 0.007 |
RMSD bond angle | 1.100 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 23.620 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.064 | 0.206 |
Number of reflections | 22407 | |
<I/σ(I)> | 7.2 | 2.8 |
Completeness [%] | 98.7 | 99.9 |
Redundancy | 6.6 | 4.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6 | PROTEIN WAS CRYSTALLISED IN 50 MM MES, PH 6.0, 0.1 M KCL, 2 MM MGCL2 AND 10 % PEG 400 AND CRYOPROTECTED IN 20 % GLYCEROL |