24UY
Crystal structure of FPP-methyltransferase PcFPPMT from Pseudomonas chlororaphis O6 in complex with SAH and GPP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE TPS 07A |
| Synchrotron site | NSRRC |
| Beamline | TPS 07A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2025-10-26 |
| Detector | DECTRIS EIGER2 S 16M |
| Wavelength(s) | 0.97624 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 68.686, 98.353, 42.315 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.160 - 1.700 |
| R-factor | 0.1957 |
| Rwork | 0.194 |
| R-free | 0.23210 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.003 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.760 |
| High resolution limit [Å] | 1.700 | 3.660 | 1.700 |
| Rmerge | 0.039 | 0.028 | 0.479 |
| Rmeas | 0.044 | 0.032 | 0.549 |
| Rpim | 0.020 | 0.015 | 0.262 |
| Total number of observations | 158970 | ||
| Number of reflections | 31615 | 3292 | 3072 |
| <I/σ(I)> | 16.7 | ||
| Completeness [%] | 98.4 | 95.7 | 97 |
| Redundancy | 5 | 4.5 | 4 |
| CC(1/2) | 0.996 | 0.998 | 0.837 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 298 | 25% PEG 3350, 0.2 M MgCl2, 0.1 M Imidazole, pH 7.5 |






