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 |