1ZXU
X-ray structure of protein from arabidopsis thaliana AT5G01750
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-05-25 |
Detector | ADSC |
Wavelength(s) | 0.97900, 0.96110 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 41.066, 57.499, 75.359 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.690 - 1.700 |
R-factor | 0.191 |
Rwork | 0.189 |
R-free | 0.23100 |
Structure solution method | MAD |
RMSD bond length | 0.020 |
RMSD bond angle | 1.723 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHARP |
Refinement software | REFMAC (refmac_5.2.0005) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.760 |
High resolution limit [Å] | 1.700 | 3.660 | 1.700 |
Rmerge | 0.080 | 0.058 | 0.454 |
Number of reflections | 20314 | ||
<I/σ(I)> | 18.016 | 4.422 | |
Completeness [%] | 100.0 | 99.9 | |
Redundancy | 13.6 | 12.9 | 11.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | BATCH SEEDING | 5.5 | 293 | 10 MG/ML PROTEIN, 25% PEG 3350, 0.2 M AMMONIUM ACETATE, 0.1 M BISTRIS, temperature 293K, pH 5.5, BATCH SEEDING |
1 | BATCH SEEDING | 5.5 | 293 | 10 MG/ML PROTEIN, 25% PEG 3350, 0.2 M AMMONIUM ACETATE, 0.1 M BISTRIS, temperature 293K, pH 5.5, BATCH SEEDING |