3TDZ
N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: Structure of a human Cul1WHB-Dcn1P-stapled acetylated Ubc12N complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2011-03-20 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 131.790, 190.210, 67.506 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.000 |
| R-factor | 0.19706 |
| Rwork | 0.196 |
| R-free | 0.22352 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3tdu |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.982 |
| 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 | 2.520 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.370 | 2.000 |
| Rmerge | 0.078 | 0.439 | |
| Number of reflections | 53080 | ||
| <I/σ(I)> | 24.9 | 2.5 | |
| Completeness [%] | 96.7 | 100 | 77.2 |
| Redundancy | 6.6 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | 21% PEG3350, 0.2M KCl, pH Unbuffered, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
