9WLU
MPXV P1L Protein D14N mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL10U2 |
| Synchrotron site | SSRF |
| Beamline | BL10U2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2025-04-11 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97853 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 114.915, 114.915, 127.506 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.360 - 2.900 |
| R-factor | 0.2547 |
| Rwork | 0.253 |
| R-free | 0.28250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.582 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.460 | 3.060 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.229 | 0.325 |
| Rmeas | 0.240 | 0.345 |
| Rpim | 0.072 | 0.112 |
| Total number of observations | 77167 | 9765 |
| Number of reflections | 7118 | 1065 |
| <I/σ(I)> | 10.4 | 6.2 |
| Completeness [%] | 96.5 | |
| Redundancy | 10.8 | 9.2 |
| CC(1/2) | 0.995 | 0.537 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 290 | 1.0 M Potassium/sodium tartrate 0.1M CHES/Sodium hydroxide 9.5 0.2M Lithium sulfate |
