2XZE
Structural basis for AMSH-ESCRT-III CHMP3 interaction
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-04-15 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9760, 0.9795 |
| Spacegroup name | P 41 |
| Unit cell lengths | 45.970, 45.970, 206.910 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 51.710 - 1.750 |
| R-factor | 0.19333 |
| Rwork | 0.192 |
| R-free | 0.22694 |
| Structure solution method | SAD |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.298 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | Auto-Rickshaw |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.850 | 1.840 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.080 | 0.640 |
| Number of reflections | 141404 | |
| <I/σ(I)> | 5.1 | 1.2 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 3.3 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | 3.3 MG/ML OF AMSH PROTEIN IN 10 MM HEPES PH 8.0, 100 MM NACL WAS MIXED WITH AN EQUAL VOLUME WELL CONDITION: 2.2 M SODIUM MALONATE,WITH 30 % GLYCEROL AS CRYO-PROTECTANT |
