6E7K
Structure of the lipoprotein lipase GPIHBP1 complex that mediates plasma triglyceride hydrolysis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID30B |
| Synchrotron site | ESRF |
| Beamline | ID30B |
| Temperature [K] | 125 |
| Detector technology | PIXEL |
| Collection date | 2017-12-09 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 101.948, 153.206, 95.783 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.410 - 2.800 |
| R-factor | 0.19738 |
| Rwork | 0.195 |
| R-free | 0.23545 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hpl |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.433 |
| Data reduction software | HKL-2000 (v716.1) |
| Data scaling software | HKL-2000 (v716.1) |
| Phasing software | PHASER (v2.7.17) |
| Refinement software | REFMAC (5.8.0230) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 95.800 | 2.900 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Number of reflections | 37662 | |
| <I/σ(I)> | 13.5 | 1.5 |
| Completeness [%] | 99.4 | 99.7 |
| Redundancy | 3.3 | 3.2 |
| CC(1/2) | 0.985 | 0.728 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 200 mM magnesium acetate, 20% PEG3350 |






