5AZ9
Crystal structure of (5-residue deleted)MBP-Tom20 fusion protein tethered with ALDH presequence via a disulfide bond
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 | 2012-04-23 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 0.9 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 160.476, 71.396, 47.538 |
Unit cell angles | 90.00, 104.91, 90.00 |
Refinement procedure
Resolution | 39.550 - 1.820 |
R-factor | 0.19391 |
Rwork | 0.192 |
R-free | 0.22705 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1anf 2v1t |
RMSD bond length | 0.019 |
RMSD bond angle | 1.895 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 1.820 |
Number of reflections | 46512 |
<I/σ(I)> | 14 |
Completeness [%] | 99.8 |
Redundancy | 3.64 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 20% PEG 3350, 0.2M Potassium nitrate |