5EMT
Human Histidine Triad Nucleotide Binding Protein 1 (hHint1)-copper complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 4.2.2 |
| Synchrotron site | ALS |
| Beamline | 4.2.2 |
| Temperature [K] | 100 |
| Detector technology | CMOS |
| Collection date | 2015-09-24 |
| Detector | RDI CMOS_8M |
| Wavelength(s) | 1.37 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 77.250, 46.220, 63.830 |
| Unit cell angles | 90.00, 94.62, 90.00 |
Refinement procedure
| Resolution | 63.620 - 1.500 |
| R-factor | 0.1482 |
| Rwork | 0.147 |
| R-free | 0.16480 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3tw2 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.864 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.9) |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.10_2155: ???)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 63.620 | 63.620 | 1.530 |
| High resolution limit [Å] | 1.500 | 8.220 | 1.500 |
| Rmerge | 0.050 | 0.031 | 0.253 |
| Rmeas | 0.052 | 0.032 | 0.263 |
| Rpim | 0.014 | 0.010 | 0.072 |
| Total number of observations | 2785 | 22760 | |
| Number of reflections | 70394 | ||
| <I/σ(I)> | 43.3 | 87.3 | 9.2 |
| Completeness [%] | 100.0 | 95.4 | 100 |
| Redundancy | 13.6 | 11.8 | 13 |
| CC(1/2) | 1.000 | 1.000 | 0.983 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | 100 mM MES, 39% PEG 8000, |
