7VMW
Crystal structure of LimF prenyltransferase bound with a peptide substrate and GSPP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL32XU |
| Synchrotron site | SPring-8 |
| Beamline | BL32XU |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-07-20 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 89.660, 48.430, 91.040 |
| Unit cell angles | 90.00, 117.87, 90.00 |
Refinement procedure
| Resolution | 40.240 - 1.930 |
| R-factor | 0.1843 |
| Rwork | 0.182 |
| R-free | 0.23160 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5tty |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.228 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.240 | 2.000 |
| High resolution limit [Å] | 1.930 | 1.930 |
| Number of reflections | 52412 | 5193 |
| <I/σ(I)> | 11.67 | |
| Completeness [%] | 100.0 | |
| Redundancy | 6.9 | |
| CC(1/2) | 0.998 | 0.508 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 283 | PEG 1500, PCB (Na propionate, Na cacodylate, bis-tris propane) buffer, magnesium chloride |
