3KKK
Y92C catalytic residue mutant of Phosphoglycerate Mutase from Plasmodium falciparum
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-1 |
| Synchrotron site | SSRL |
| Beamline | BL9-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-12-20 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 0.91837 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 71.062, 76.120, 101.680 |
| Unit cell angles | 90.00, 99.68, 90.00 |
Refinement procedure
| Resolution | 31.460 - 2.080 |
| R-factor | 0.198 |
| Rwork | 0.196 |
| R-free | 0.23600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1xq9 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.930 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (refmac_5.5.0096) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.150 |
| High resolution limit [Å] | 2.080 | 2.080 |
| Rmerge | 0.055 | 0.599 |
| Number of reflections | 64085 | |
| <I/σ(I)> | 10.5 | 1.22 |
| Completeness [%] | 99.5 | 99.8 |
| Redundancy | 2.6 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 298 | 35% PEG 1000, 0.1 M HEPES pH 7.2, 0.1 M KSCN, 5 mM DTT, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
