3LVJ
Crystal Structure of E.coli IscS-TusA complex (form 1)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 31-ID |
| Synchrotron site | APS |
| Beamline | 31-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-11 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.9793 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 72.299, 106.545, 122.106 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.646 - 2.435 |
| R-factor | 0.223 |
| Rwork | 0.222 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1P3W and 1DCJ |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.675 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.6_289) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.540 |
| High resolution limit [Å] | 2.435 | 5.280 | 2.450 |
| Rmerge | 0.072 | 0.032 | 0.365 |
| Number of reflections | 34585 | ||
| <I/σ(I)> | 13.1 | ||
| Completeness [%] | 96.4 | 99.6 | 79 |
| Redundancy | 5.9 | 6.9 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 295 | 20% PEG 3350, 0.12M Magnisum Formate, vapor diffusion, sitting drop, temperature 295K |
