2IF4
Crystal structure of a multi-domain immunophilin from Arabidopsis thaliana
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 | 2004-07-20 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.934 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 86.142, 117.873, 40.112 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.850 |
R-factor | 0.296 |
Rwork | 0.290 |
R-free | 0.35500 |
Structure solution method | MIRAS |
RMSD bond length | 0.008 |
RMSD bond angle | 1.546 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | MLPHARE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.920 |
High resolution limit [Å] | 2.850 | 2.850 |
Rmerge | 0.050 | 0.430 |
Number of reflections | 9813 | |
<I/σ(I)> | 20 | 2.6 |
Completeness [%] | 98.0 | 96.9 |
Redundancy | 3.5 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.3 | 290 | 2.3 M ammonium sulfate, 2% (v/v) PEG 400, 0.1 M Hepes, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 290K |