3G1N
Catalytic domain of the human E3 ubiquitin-protein ligase HUWE1
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-01-21 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 176.530, 72.213, 77.238 |
Unit cell angles | 90.00, 106.94, 90.00 |
Refinement procedure
Resolution | 29.300 - 2.600 |
R-factor | 0.21726 |
Rwork | 0.214 |
R-free | 0.27919 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1nd7 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.195 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0063) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 28536 | |
<I/σ(I)> | 10.851 | 1.96 |
Completeness [%] | 98.9 | 91.8 |
Redundancy | 3.5 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 15% PEG-4000, 10% ISOPROPANOL, 0.1 M TRIS BUFFER, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |