5M3N
HTRA2 wild-type structure
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-3 |
Synchrotron site | ESRF |
Beamline | ID14-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-02-25 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.931 |
Spacegroup name | H 3 |
Unit cell lengths | 82.828, 82.828, 127.415 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.633 - 1.649 |
R-factor | 0.1494 |
Rwork | 0.147 |
R-free | 0.17550 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1lcy |
RMSD bond length | 0.010 |
RMSD bond angle | 1.013 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX ((1.10_2155: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.633 | 1.740 |
High resolution limit [Å] | 1.649 | 1.650 |
Rmerge | 0.055 | |
Number of reflections | 38703 | |
<I/σ(I)> | 18.9 | |
Completeness [%] | 98.7 | |
Redundancy | 5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6 | 293 | Crystals were grown using the sitting drop vapor-diffusion method by mixing equal volumes of protein (10-15 mg/mL) and reservoir solution containing 0.1 M MES pH 6.0, 1 M LiCl, and 15-20% (w/v) PEG-6000 |