4MDR
Crystal structure of adaptor protein complex 4 (AP-4) mu4 subunit C-terminal domain D190A mutant, in complex with a sorting peptide from the amyloid precursor protein (APP)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-11-01 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.507, 56.729, 60.180 |
| Unit cell angles | 90.00, 106.67, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.850 |
| R-factor | 0.216 |
| Rwork | 0.213 |
| R-free | 0.25960 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3l81 |
| RMSD bond length | 0.022 |
| RMSD bond angle | 2.046 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.910 |
| High resolution limit [Å] | 1.840 | 1.840 |
| Rmerge | 0.077 | 0.350 |
| Number of reflections | 25043 | |
| <I/σ(I)> | 15.8 | 2.7 |
| Completeness [%] | 97.1 | 75.5 |
| Redundancy | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 295 | 15% PEG 6000, 3% trimethylamine N-oxide dihydrate, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K |
