5KM0
Human Histidine Triad Nucleotide Binding Protein 1 (hHint) IMP complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-12-15 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 64.325, 89.589, 46.372 |
| Unit cell angles | 90.00, 90.03, 90.00 |
Refinement procedure
| Resolution | 41.182 - 1.533 |
| R-factor | 0.1899 |
| Rwork | 0.188 |
| R-free | 0.22330 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1kpc |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.108 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.8.4_1496) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 64.325 | 89.589 | 1.538 |
| High resolution limit [Å] | 1.533 | 7.113 | 1.533 |
| Rmerge | 0.058 | 0.309 | |
| Number of reflections | 77524 | ||
| <I/σ(I)> | 9.2 | ||
| Completeness [%] | 98.5 | 98.8 | 83 |
| Redundancy | 3.2 | 3 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.7 | 293 | 100 mM MES, 34% PEG 8000 |
