3DB4
Crystal structure of the tandem tudor domains of the E3 ubiquitin-protein ligase UHRF1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-03-05 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.00000 |
Spacegroup name | P 62 |
Unit cell lengths | 98.654, 98.654, 43.345 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 38.660 - 2.400 |
R-factor | 0.22008 |
Rwork | 0.217 |
R-free | 0.28462 |
Structure solution method | SAD |
RMSD bond length | 0.007 |
RMSD bond angle | 1.055 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.660 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Number of reflections | 9579 | |
<I/σ(I)> | 25.55 | 4.76 |
Completeness [%] | 99.7 | 97.4 |
Redundancy | 11.9 | 10.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 10 % PEG 8000, 0.1 M SODIUM CACODYLATE, 0.2 M AMMONIUM SULFATE, 0.001 M TCEP, pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 298K |