4EQE
Crystal structure of histidine triad nucleotide-binding protein 1 (HINT1) from human complexed with Lys-AMS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-07-06 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.033 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 79.001, 46.409, 64.225 |
| Unit cell angles | 90.00, 95.46, 90.00 |
Refinement procedure
| Resolution | 24.396 - 1.520 |
| R-factor | 0.1431 |
| Rwork | 0.142 |
| R-free | 0.16220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6rhn |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.189 |
| 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 | 1.570 |
| High resolution limit [Å] | 1.520 | 3.270 | 1.520 |
| Rmerge | 0.048 | 0.026 | 0.299 |
| Number of reflections | 35542 | ||
| <I/σ(I)> | 13.2 | ||
| Completeness [%] | 99.3 | 99.9 | 98.2 |
| Redundancy | 7.5 | 7.4 | 6.5 |
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 |
