3TW2
High resolution structure of human histidine triad nucleotide-binding protein 1 (hHINT1)/AMP complex in a monoclinic space group
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-07-08 |
| Detector | MAR CCD 165 mm |
| Wavelength(s) | 0.8123 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 77.421, 46.449, 64.034 |
| Unit cell angles | 90.00, 94.42, 90.00 |
Refinement procedure
| Resolution | 25.580 - 1.380 |
| R-factor | 0.12277 |
| Rwork | 0.121 |
| R-free | 0.16148 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kpf |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.479 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.580 | 1.450 |
| High resolution limit [Å] | 1.380 | 1.380 |
| Rmerge | 0.122 | 0.291 |
| Number of reflections | 45932 | |
| <I/σ(I)> | 13.1 | 3.4 |
| Completeness [%] | 100.0 | 84 |
| Redundancy | 4.4 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 278 | 19% PEG 8000, 0.1M sodium cacodylate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 278K |
