3H13
c-FLIPL protease-like domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-04-09 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.1 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 101.940, 101.940, 61.360 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.430 - 2.200 |
R-factor | 0.187 |
Rwork | 0.187 |
R-free | 0.22000 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.012 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | CNS (1.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.280 |
High resolution limit [Å] | 2.200 | 2.200 |
Number of reflections | 19006 | |
<I/σ(I)> | 19.4 | 6.8 |
Completeness [%] | 99.9 | 100 |
Redundancy | 6.4 | 6.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 290 | 0.1 M Mes, 18% PEG, 5000 monomethyl ether, 0.1 M ammonium sulfate , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |