6XHC
Structure of glycinyl 5'-O-adenosine phosphoramidate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2019-02-17 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97856 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 100.756, 32.686, 72.723 |
| Unit cell angles | 90.00, 90.46, 90.00 |
Refinement procedure
| Resolution | 41.600 - 1.600 |
| R-factor | 0.1862 |
| Rwork | 0.184 |
| R-free | 0.23740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | AFK1 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.345 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.660 |
| High resolution limit [Å] | 1.600 | 3.450 | 1.600 |
| Rmerge | 0.055 | 0.032 | 0.775 |
| Rmeas | 0.060 | 0.035 | 0.858 |
| Rpim | 0.024 | 0.014 | 0.363 |
| Total number of observations | 184557 | ||
| Number of reflections | 31715 | 3309 | 3137 |
| <I/σ(I)> | 10.2 | ||
| Completeness [%] | 99.4 | 99.7 | 98.9 |
| Redundancy | 5.8 | 6 | 5.4 |
| CC(1/2) | 0.999 | 0.680 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 291 | PROTEIN WAS CRYSTALLIZED FROM 25%, PEG 3350, 20 MM SODIUM CITRATE, PH 5.5, Glycinyl-O5'-adenosine phosphoramidate was soaked into the crystals using a stock solution of 100 mM, to achieve ~35 mM in the soaking solution |
