5KLY
Human Histidine Triad Nucleotide Binding Protein 1 (hHint1) H112N mutant adenosine nucleoside phosphoramidate substrate 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) | 1.000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 77.865, 46.502, 64.063 |
| Unit cell angles | 90.00, 94.80, 90.00 |
Refinement procedure
| Resolution | 63.838 - 1.300 |
| R-factor | 0.1496 |
| Rwork | 0.148 |
| R-free | 0.17110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3tw2 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.966 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.9) |
| Phasing software | PHASER (2.6.0) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 63.840 | 63.840 | 1.320 |
| High resolution limit [Å] | 1.300 | 7.120 | 1.300 |
| Rmerge | 0.049 | 0.022 | 0.262 |
| Rmeas | 0.058 | ||
| Rpim | 0.030 | ||
| Total number of observations | 195307 | ||
| Number of reflections | 53994 | ||
| <I/σ(I)> | 19 | ||
| Completeness [%] | 96.0 | 89.5 | 93.8 |
| Redundancy | 3.6 | 3.4 | 3.5 |
| CC(1/2) | 0.999 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.4 | 293 | 100 mM MES, 32% PEG 8000 |
