7LRZ
Structure of the Human ALK GRD
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-08-19 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0332 |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 76.141, 76.141, 230.850 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 43.430 - 1.910 |
| R-factor | 0.1893 |
| Rwork | 0.188 |
| R-free | 0.21430 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7lir |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.297 |
| Data reduction software | XDS (20200417) |
| Data scaling software | SCALA (0.7.4) |
| Phasing software | PHASER (2.8.3) |
| Refinement software | PHENIX (dev_3915) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 43.430 | 43.430 | 1.960 |
| High resolution limit [Å] | 1.910 | 8.980 | 1.910 |
| Rmerge | 0.147 | 0.049 | 0.786 |
| Rmeas | 0.151 | 0.051 | 1.008 |
| Rpim | 0.036 | 0.013 | 0.620 |
| Total number of observations | 475077 | 5925 | 2809 |
| Number of reflections | 30911 | 407 | 1408 |
| <I/σ(I)> | 13.1 | 36.1 | 0.7 |
| Completeness [%] | 97.8 | 99.3 | 69.3 |
| Redundancy | 15.4 | 14.6 | 2 |
| CC(1/2) | 0.998 | 0.999 | 0.685 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | 289.15 | Imidazole pH 8.0, 10% PEG 8000, 0.2 M Ca(OAc)2 |
