5D94
Crystal structure of LC3-LIR peptide complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44XU |
Synchrotron site | SPring-8 |
Beamline | BL44XU |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-10-15 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 0.9 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 40.724, 39.162, 42.756 |
Unit cell angles | 90.00, 115.05, 90.00 |
Refinement procedure
Resolution | 19.580 - 1.530 |
R-factor | 0.17672 |
Rwork | 0.175 |
R-free | 0.21473 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.016 |
RMSD bond angle | 1.821 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.560 |
High resolution limit [Å] | 1.530 | 1.530 |
Rmerge | 0.052 | 0.098 |
Number of reflections | 17994 | |
<I/σ(I)> | 49.7 | |
Completeness [%] | 96.4 | 97.9 |
Redundancy | 3.6 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1M Potassium thiocyanate, 30%(w/v) Polyethylene glycol monomethyl ether 2000 |