3AX3
Crystal structure of rat TOM20-ALDH presequence complex: a complex (form2) between Tom20 and a disulfide-bridged presequence peptide containing D-Cys and L-Cys at the i and i+3 positions.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-5A |
| Synchrotron site | Photon Factory |
| Beamline | BL-5A |
| Temperature [K] | 95 |
| Detector technology | CCD |
| Collection date | 2008-06-25 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 1.00 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 99.596, 99.596, 195.180 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 28.940 - 2.100 |
| R-factor | 0.2452 |
| Rwork | 0.243 |
| R-free | 0.28698 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1WT4 2v1t |
| RMSD bond length | 0.024 |
| RMSD bond angle | 2.006 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER (MR) |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 4.520 | 2.100 |
| Rmerge | 0.045 | 0.496 | |
| Number of reflections | 22101 | ||
| Completeness [%] | 99.7 | 97 | 100 |
| Redundancy | 9.3 | 9.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 0.1M Tris-HCl pH8.0, 0.2M MgCl2, 30% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
