3L4H
Helical box domain and second WW domain of the human E3 ubiquitin-protein ligase HECW1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-12-16 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97899 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 26.079, 44.082, 39.610 |
| Unit cell angles | 90.00, 92.54, 90.00 |
Refinement procedure
| Resolution | 29.450 - 1.800 |
| R-factor | 0.15228 |
| Rwork | 0.150 |
| R-free | 0.19956 |
| Structure solution method | SAD |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.546 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Number of reflections | 8513 | |
| <I/σ(I)> | 31.0366 | 5.462 |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 4.9 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 291.1 | equal volumes of protein (10 mg/ml) [containing 0.1 MM actetic acid PH 3.0] was mixed with crystallization buffer (1.0 M sodium citrate, 0.1 MM immidazole PH 8.0), along with trypsin at a concentration of 1 mg trypsin/500 mg protein. cryoprotected with 15% glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 291.1K |
