3N90
The 1.7 Angstrom resolution crystal structure of AT2G44920, a pentapeptide repeat protein from Arabidopsis thaliana thylakoid lumen.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-12-11 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.979 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 59.064, 75.444, 59.901 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.700 |
R-factor | 0.2279 |
Rwork | 0.226 |
R-free | 0.25851 |
Structure solution method | SAD |
RMSD bond length | 0.015 |
RMSD bond angle | 1.593 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.790 |
High resolution limit [Å] | 1.700 | 1.700 |
Number of reflections | 14963 | |
<I/σ(I)> | 40.84 | 18.9 |
Completeness [%] | 99.2 | 100 |
Redundancy | 1.87 | 1.92 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.2 | 293 | well buffer: 2.5M ammonium sulfate, 0.5M sodium acetate; Sample buffer: 0.25M sodium chloride, 10% glycerol, 0.02M Tris, pH 7.8 protein concentration=15mg/mL, VAPOR DIFFUSION, HANGING DROP, temperature 293K |