8VR7
crystal structure of the Pcryo_0619 N-acetyltransferase from Psychrobacter cryohalolentis K5 int he presence of acetyl coenzyme A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SEALED TUBE |
| Source details | BRUKER D8 QUEST |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-11-19 |
| Detector | Bruker PHOTON II |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 107.895, 157.818, 66.046 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.690 - 1.900 |
| R-factor | 0.19948 |
| Rwork | 0.197 |
| R-free | 0.23993 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.366 |
| Data reduction software | SAINT |
| Data scaling software | SADABS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0405) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Number of reflections | 89307 | 12536 |
| <I/σ(I)> | 14.3 | 2.8 |
| Completeness [%] | 99.7 | 99.2 |
| Redundancy | 11.5 | 5.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | Protein incubated with 3 mM acetyl-CoA. Precipitant: 8-12% PEG 8000 and 100 mM homopipes (pH 5) |
