2OMG
Structure of human insulin cocrystallized with protamine and urea
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-5 |
| Synchrotron site | MAX II |
| Beamline | I911-5 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-01-23 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.969 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 61.660, 61.660, 85.540 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.880 - 1.520 |
| R-factor | 0.18391 |
| Rwork | 0.183 |
| R-free | 0.20947 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | insulin trimer R-conformation |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.545 |
| 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 | 1.600 |
| High resolution limit [Å] | 1.520 | 1.520 |
| Rmerge | 0.082 | 0.330 |
| Number of reflections | 25119 | |
| <I/σ(I)> | 14.4 | 4.9 |
| Completeness [%] | 93.0 | 74.7 |
| Redundancy | 8 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.3 | 291 | 60mM m-cresol, 3M urea, 1.0 mg/ml protamine sulphate, 400mM NaCl, 40mM phosphate buffer, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
