9LPT
Structure of the P113 protein from Plasmodium falciparum
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL18U1 |
| Synchrotron site | SSRF |
| Beamline | BL18U1 |
| Temperature [K] | 291.15 |
| Detector technology | PIXEL |
| Collection date | 2017-03-29 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.97914 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 72.920, 72.920, 143.280 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 26.340 - 1.700 |
| R-factor | 0.1903 |
| Rwork | 0.189 |
| R-free | 0.22120 |
| Structure solution method | MAD |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.350 |
| Data reduction software | HKL-2000 |
| Data scaling software | xia2 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.620 | 5.000 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.129 | |
| Number of reflections | 49135 | 49135 |
| <I/σ(I)> | 15.6 | |
| Completeness [%] | 100.0 | |
| Redundancy | 3.7 | |
| CC(1/2) | 0.998 | 0.998 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291.15 | 0.5 mM MES, 22% PEG3350 |






