2FGE
Crystal structure of presequence protease PreP from Arabidopsis thaliana
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-11-06 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.9792 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 110.834, 114.332, 162.984 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 93.660 - 2.100 |
R-factor | 0.209 |
Rwork | 0.206 |
R-free | 0.25600 |
Structure solution method | SAD |
RMSD bond length | 0.011 |
RMSD bond angle | 1.311 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELXS |
Refinement software | REFMAC (5.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 93.660 | 2.140 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.119 | 0.417 |
Number of reflections | 116872 | |
<I/σ(I)> | 10.4 | 2.26 |
Completeness [%] | 96.5 | 86.6 |
Redundancy | 4.7 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | 22% PEG 6000, 0.1M Hepes, 0.025M magnesium chloride, 0.1% beta-mercaptoethanol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |