6UMG
Crystal structure of erenumab Fab bound to the extracellular domain of CGRP receptor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU FR-E SUPERBRIGHT |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-05-26 |
| Detector | RIGAKU SATURN 92 |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 70.464, 112.520, 77.254 |
| Unit cell angles | 90.00, 91.84, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.700 |
| R-factor | 0.2466 |
| Rwork | 0.245 |
| R-free | 0.28190 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n7p |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.899 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 5.800 | 2.700 |
| Rmerge | 0.140 | 0.068 | 0.593 |
| Rmeas | 0.165 | 0.080 | 0.704 |
| Rpim | 0.088 | 0.043 | 0.376 |
| Number of reflections | 33135 | 3346 | 3274 |
| <I/σ(I)> | 5.6 | 2.07 | |
| Completeness [%] | 99.9 | 98.8 | 99.9 |
| Redundancy | 3.4 | 3.4 | 3.3 |
| CC(1/2) | 0.995 | 0.698 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.12 M ethylene glycols, 0.1 M HEPES:MOPS, pH 7.5, 37.5% MPD + PEG1000 + PEG3350 |
