5KGN
1.95A resolution structure of independent phosphoglycerate mutase from C. elegans in complex with a macrocyclic peptide inhibitor (2d)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 17-ID |
| Synchrotron site | APS |
| Beamline | 17-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-04-10 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.00000 |
| Spacegroup name | P 1 2 1 |
| Unit cell lengths | 73.782, 75.832, 101.420 |
| Unit cell angles | 90.00, 95.66, 90.00 |
Refinement procedure
| Resolution | 35.490 - 1.950 |
| R-factor | 0.156 |
| Rwork | 0.154 |
| R-free | 0.20400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5kgl |
| RMSD bond length | 0.017 |
| RMSD bond angle | 0.897 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.24) |
| Phasing software | PHASER (2.6.1) |
| Refinement software | PHENIX |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.170 | 1.990 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.146 | 0.603 |
| Number of reflections | 80429 | |
| <I/σ(I)> | 7.8 | |
| Completeness [%] | 99.0 | 98.1 |
| Redundancy | 3.4 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 30% (w/v) PEG 4000, 0.1 Tris, 0.2 M magnesium chloride |
