7TU1
Structure of the L. blandensis dGTPase R37A mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-11-01 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 181.437, 181.437, 110.845 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.210 - 1.800 |
| R-factor | 0.1771 |
| Rwork | 0.177 |
| R-free | 0.19900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3bg2 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.933 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 1.910 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.124 | 1.882 |
| Rmeas | 0.128 | 1.948 |
| Number of reflections | 169361 | 26929 |
| <I/σ(I)> | 11.31 | 1.01 |
| Completeness [%] | 99.7 | 99.1 |
| Redundancy | 15.1 | 15 |
| CC(1/2) | 0.995 | 0.547 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | Crystal grown in 1ul:1ul drops of well solution (0.6M Sodium Potassium Tartrate, 0.16M Lithium Sulfate, 0.1M Bis-Tris pH 6.5) and 10mg/mL protein. Cryoprotected by soaking in well solution with 30% ethylene glycol added |
