2OMP
LYQLEN peptide derived from human insulin chain A, residues 13-18
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID13 |
| Synchrotron site | ESRF |
| Beamline | ID13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-07-16 |
| Detector | MAR CCD 165 mm |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 9.666, 28.003, 17.346 |
| Unit cell angles | 90.00, 96.24, 90.00 |
Refinement procedure
| Resolution | 17.240 - 1.900 |
| R-factor | 0.191 |
| Rwork | 0.189 |
| R-free | 0.22800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | idealized beta strands polyalanine |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.357 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 90.000 | 90.000 | 1.940 |
| High resolution limit [Å] | 1.800 | 3.080 | 1.800 |
| Rmerge | 0.186 | 0.130 | 0.402 |
| Number of reflections | 752 | ||
| <I/σ(I)> | 4.8 | ||
| Completeness [%] | 91.0 | 95.2 | 83.5 |
| Redundancy | 2.1 | 2.3 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 2.5 | 310 | 20mM peptide in 100 mM NaCl and 50 mM phosphate, pH 2.5, VAPOR DIFFUSION, HANGING DROP, temperature 310K |
