2JK3
CRYSTAL STRUCTURE OF THE HLYIIR MUTANT PROTEIN WITH RESIDUES 169-186 SUBSTITUTED BY GSSGSSG LINKER
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-03-08 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 38.383, 78.990, 143.814 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.000 - 2.200 |
| R-factor | 0.201 |
| Rwork | 0.198 |
| R-free | 0.25400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2fx0 |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.504 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.4.0077) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.080 | 0.580 |
| Number of reflections | 22752 | |
| <I/σ(I)> | 15.8 | 1.9 |
| Completeness [%] | 98.7 | 91.4 |
| Redundancy | 4.1 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | TRIS, PEG3350, AMMONIUM SULFATE, pH 7.5 |
