2WZD
The catalytically active fully closed conformation of human phosphoglycerate kinase K219A mutant in complex with ADP, 3PG and aluminium trifluoride
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-01-22 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 39.380, 91.590, 108.480 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.560 |
| R-factor | 0.16815 |
| Rwork | 0.166 |
| R-free | 0.20181 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3c39 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.646 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0070) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.640 |
| High resolution limit [Å] | 1.560 | 1.560 |
| Rmerge | 0.060 | 0.280 |
| Number of reflections | 55495 | |
| <I/σ(I)> | 10.9 | 3.7 |
| Completeness [%] | 98.0 | 95.9 |
| Redundancy | 2.7 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 22% PEG2000MME, 0.1M BIS/TRIS PH 6.5 |
