5AZ6
Crystal structure of MBP-Tom20 fusion protein with a 2-residue spacer in the connector helix
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL32XU |
| Synchrotron site | SPring-8 |
| Beamline | BL32XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-06-24 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 129.906, 81.227, 109.890 |
| Unit cell angles | 90.00, 106.38, 90.00 |
Refinement procedure
| Resolution | 24.720 - 2.560 |
| R-factor | 0.20625 |
| Rwork | 0.203 |
| R-free | 0.25972 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1anf 2v1t |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.718 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.560 |
| Number of reflections | 35889 |
| <I/σ(I)> | 11 |
| Completeness [%] | 99.9 |
| Redundancy | 3.79 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.3 | 293 | 16% PEG 3350, 0.2M Disodium malonate, 0.1M HEPES (pH7.3) |
