4I1F
Structure of Parkin-S223P E3 ligase
Experimental procedure
Experimental method | MAD |
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 | 2012-06-06 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.2831, 1.2699 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 86.955, 133.155, 65.385 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 72.810 - 1.580 |
R-factor | 0.20706 |
Rwork | 0.205 |
R-free | 0.24528 |
Structure solution method | MAD |
RMSD bond length | 0.025 |
RMSD bond angle | 2.260 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SHELX |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 73.000 | 1.670 |
High resolution limit [Å] | 1.580 | 1.580 |
Rmerge | 0.990 | |
Number of reflections | 52033 | |
<I/σ(I)> | 11 | 1.6 |
Completeness [%] | 98.5 | 99.8 |
Redundancy | 6.9 | 6.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 283 | 0.1 M HEPES, pH 7.5, 20% PEG4000, 10% isopropanol, 10 mM barium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 283K |