5J3H
Human insulin receptor domains L1-CR in complex with peptide S519C16 and 83-7 Fv
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-07-01 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 176.776, 176.776, 86.186 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.790 - 3.270 |
| R-factor | 0.2272 |
| Rwork | 0.226 |
| R-free | 0.24840 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4oga |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.230 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.10.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.790 | 3.390 |
| High resolution limit [Å] | 3.270 | 3.270 |
| Rmerge | 2.230 | |
| Number of reflections | 21483 | |
| <I/σ(I)> | 7.68 | 1 |
| Completeness [%] | 99.4 | 98.9 |
| Redundancy | 6.3 | 6.38 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 300 | 1.75 M (NH4)2HPO4 |
