5IPC
Human Histidine Triad Nucleotide Binding Protein 1 (hHint1) H112N mutant nucleoside thiophosphoramidate substrate 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 | 2015-04-18 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 77.943, 46.504, 63.916 |
| Unit cell angles | 90.00, 94.72, 90.00 |
Refinement procedure
| Resolution | 33.188 - 1.300 |
| R-factor | 0.1527 |
| Rwork | 0.152 |
| R-free | 0.16980 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3tw2 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.995 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 63.699 | 63.699 | 1.304 |
| High resolution limit [Å] | 1.300 | 6.032 | 1.300 |
| Rmerge | 0.034 | 0.021 | 0.249 |
| Rmeas | 0.026 | 0.300 | |
| Rpim | 0.014 | 0.165 | |
| Total number of observations | 1844 | 1716 | |
| Number of reflections | 54978 | ||
| <I/σ(I)> | 19.3 | 41.7 | 4.6 |
| Completeness [%] | 97.9 | 97.5 | 96.1 |
| Redundancy | 3.3 | 3.1 | 3.2 |
| CC(1/2) | 0.999 | 0.998 | 0.944 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6.5 | 293 | 100 mM MES, 37% PEG 8000 |
