5Z43
Crystal structure of prenyltransferase AmbP1 apo structure
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-1A |
| Synchrotron site | Photon Factory |
| Beamline | BL-1A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-12-09 |
| Detector | DECTRIS PILATUS 2M-F |
| Wavelength(s) | 1.1000 |
| Spacegroup name | P 41 |
| Unit cell lengths | 116.263, 116.263, 48.723 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.105 - 2.361 |
| R-factor | 0.1939 |
| Rwork | 0.190 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5yk9 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.973 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.13_2998: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.900 | 2.450 |
| High resolution limit [Å] | 2.360 | 2.360 |
| Rmerge | 0.038 | 0.493 |
| Number of reflections | 27028 | 2823 |
| <I/σ(I)> | 18.8 | 2.3 |
| Completeness [%] | 99.6 | 99.2 |
| Redundancy | 3.9 | 3.9 |
| CC(1/2) | 0.999 | 0.807 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 100mM MES (pH6.5), 0.2M MgCl2, 22% PEG8000 |






