4EQH
Crystal structure of histidine triad nucleotide-binding protein 1 (HINT1) from human complexed with Trp-AMS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-07-06 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 79.000, 46.427, 63.884 |
| Unit cell angles | 90.00, 95.24, 90.00 |
Refinement procedure
| Resolution | 24.348 - 1.668 |
| R-factor | 0.145 |
| Rwork | 0.143 |
| R-free | 0.17290 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6rhn |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.250 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.7.1_743) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 25.000 | 25.000 | 1.730 |
| High resolution limit [Å] | 1.668 | 3.590 | 1.668 |
| Rmerge | 0.053 | 0.021 | 0.489 |
| Number of reflections | 26559 | ||
| <I/σ(I)> | 9.7 | ||
| Completeness [%] | 98.4 | 99.7 | 96.7 |
| Redundancy | 7.5 | 7.4 | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | 25-28% PEG3350, 0.1 M HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
