2X15
The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with ADP and 1,3- bisphosphoglycerate
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 | 2009-05-06 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 38.730, 91.750, 108.310 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.100 |
| R-factor | 0.19488 |
| Rwork | 0.192 |
| R-free | 0.23795 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2wzb |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.401 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0070) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.210 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.080 | 0.320 |
| Number of reflections | 22995 | |
| <I/σ(I)> | 10.2 | 3 |
| Completeness [%] | 99.1 | 99.8 |
| Redundancy | 2.8 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | 0.1M BIS/TRIS PH 6.5, 21% P2000MME |
