3TDU
N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: Structure of a human Cul1WHB-Dcn1P-acetylated Ubc12N complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2010-12-09 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 135.431, 65.454, 64.182 |
| Unit cell angles | 90.00, 104.73, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.500 |
| R-factor | 0.20738 |
| Rwork | 0.206 |
| R-free | 0.23249 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ldj |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.915 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CCP4 |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.040 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.890 | 1.500 |
| Rmerge | 0.090 | 0.413 | |
| Number of reflections | 78739 | ||
| <I/σ(I)> | 2.6 | ||
| Completeness [%] | 96.2 | 97.1 | 88 |
| Redundancy | 3.7 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4 | 276 | 27% PEG1500, 0.1M MIB, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 276K |
