3MK4
X-Ray structure of human PEX3 in complex with a PEX19 derived peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-12-18 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.91841 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.470, 65.670, 61.580 |
| Unit cell angles | 90.00, 91.53, 90.00 |
Refinement procedure
| Resolution | 24.970 - 2.420 |
| R-factor | 0.19634 |
| Rwork | 0.194 |
| R-free | 0.23368 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | unrefined model of PEX3 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.081 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.480 |
| High resolution limit [Å] | 2.420 | 2.420 |
| Rmerge | 0.108 | 0.680 |
| Number of reflections | 11779 | |
| <I/σ(I)> | 20.2 | 3 |
| Completeness [%] | 99.7 | 99.8 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | 24% PEG 3350, 0.1M Bis-Tris, 0.2M NaCl, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
