2JJ7
Crystal structure of the HlyIIR mutant protein with residues 170-185 substituted by alanine
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-01-30 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 66.831, 120.414, 55.178 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 25.000 - 2.100 |
| R-factor | 0.181 |
| Rwork | 0.179 |
| R-free | 0.23700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2fx0 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.101 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.4.0065) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.180 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.070 | 0.500 |
| Number of reflections | 26373 | |
| <I/σ(I)> | 15 | 1.8 |
| Completeness [%] | 97.6 | 86.1 |
| Redundancy | 4.8 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | TRIS, AMMONIUM SULFATE, PEG3350, pH 7.5 |
