6RMW
Structure of N-terminal truncated IMP bound Plasmodium falciparum IMP-nucleotidase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID30B |
| Synchrotron site | ESRF |
| Beamline | ID30B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-12-09 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 107.800, 203.900, 115.300 |
| Unit cell angles | 90.00, 113.40, 90.00 |
Refinement procedure
| Resolution | 48.073 - 3.500 |
| R-factor | 0.2386 |
| Rwork | 0.236 |
| R-free | 0.27900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6rmd |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.451 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.16_3549: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.700 | 4.300 |
| High resolution limit [Å] | 3.500 | 3.500 |
| Number of reflections | 57015 | 26211 |
| <I/σ(I)> | 4.2 | |
| Completeness [%] | 99.1 | |
| Redundancy | 6.7 | |
| CC(1/2) | 0.760 | 0.767 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 292 | 0.1 M HEPES pH 7.5, 0.2 M calcium acetate, 10% (w/v) PEG 8000 by co-crystallizing the protein with 5 mM of IMP |
