6ITO
Crystal structure of pyruvate kinase (PYK) from Mycobacterium tuberculosis in complex with Oxalate, AMP and inhibitor Ribose 5-Phosphate
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-09-03 |
| Detector | DECTRIS PILATUS 2M-F |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 31 |
| Unit cell lengths | 125.550, 125.550, 143.821 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 62.770 - 2.550 |
| R-factor | 0.20773 |
| Rwork | 0.206 |
| R-free | 0.24762 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5wsc |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.219 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0232) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 62.770 | 2.600 |
| High resolution limit [Å] | 2.550 | 2.550 |
| Rmerge | 0.124 | 0.940 |
| Number of reflections | 82657 | 4510 |
| <I/σ(I)> | 8.8 | 1.6 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 4 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.2 | 277 | 12% PEG 8000, 20% glycerol, 50 mM triethanolamine-HCl (TEA) buffer pH 7.2, 100 mM KCl, 50 mM MgCl2, 5 mM oxalate, 5 mM AMP, 5 mM D-ribose 5-phosphate |
