3PUK
Re-refinement of the crystal structure of Munc18-3 and Syntaxin4 N-peptide complex
Replaces: 2PJXExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-06-06 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.115872 |
| Spacegroup name | P 21 3 |
| Unit cell lengths | 170.400, 170.400, 170.400 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.541 - 3.054 |
| R-factor | 0.2407 |
| Rwork | 0.239 |
| R-free | 0.27900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | SQUID SEC1 PDB ENTRY 1EPU |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.602 |
| Data reduction software | DENZO |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.160 |
| High resolution limit [Å] | 3.050 | 3.050 |
| Rmerge | 0.065 | 0.980 |
| Number of reflections | 31147 | |
| <I/σ(I)> | 15 | 1.7 |
| Completeness [%] | 98.8 | 100 |
| Redundancy | 6.3 | 5.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 10-13% PEG 3350, 0.2M MGACETATE, 0.1M MES, PH6.5, 50MM MGCL2, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
