4EQG
Crystal structure of histidine triad nucleotide-binding protein 1 (HINT1) from human complexed with Ala-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 | 78.309, 46.374, 64.105 |
| Unit cell angles | 90.00, 95.02, 90.00 |
Refinement procedure
| Resolution | 25.839 - 1.520 |
| R-factor | 0.1422 |
| Rwork | 0.141 |
| R-free | 0.16420 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6rhn |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.242 |
| 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] | 50.000 | 50.000 | 1.570 |
| High resolution limit [Å] | 1.520 | 3.270 | 1.520 |
| Rmerge | 0.039 | 0.028 | 0.115 |
| Number of reflections | 34800 | ||
| <I/σ(I)> | 20.7 | ||
| Completeness [%] | 98.4 | 98.4 | 97.1 |
| Redundancy | 7.5 | 7.4 | 6.7 |
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 |
