2OMH
Structure of human insulin cocrystallized with ARG-12 peptide in presence of urea
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-2 |
| Synchrotron site | MAX II |
| Beamline | I911-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-10-07 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 61.360, 61.360, 85.600 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 14.950 - 1.360 |
| R-factor | 0.20136 |
| Rwork | 0.200 |
| R-free | 0.22274 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | insulin trimer R conformation |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.112 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.400 |
| High resolution limit [Å] | 1.360 | 1.360 |
| Rmerge | 0.058 | 0.610 |
| Number of reflections | 34738 | |
| <I/σ(I)> | 12.3 | 2.2 |
| Completeness [%] | 96.9 | 98.8 |
| Redundancy | 5.3 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.3 | 291 | 500mM NaCl, 2.5M urea, 1.2mg/ml ARG-12 peptide, 50mM resorcinol, 50mM phosphate buffer, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
