2B3X
Structure of an orthorhombic crystal form of human cytosolic aconitase (IRP1)
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-02-26 |
Detector | MARRESEARCH |
Wavelength(s) | 1.741, 1.739, 1.283 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 75.352, 103.307, 225.957 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 113.230 - 2.540 |
Rwork | 0.180 |
R-free | 0.22500 |
Structure solution method | MAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.230 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | SHARP |
Refinement software | REFMAC (5.2.0003) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 113.230 |
High resolution limit [Å] | 2.540 |
Rmerge | 0.079 |
Number of reflections | 28614 |
<I/σ(I)> | 11.1 |
Completeness [%] | 94.6 |
Redundancy | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | VAPOR DIFFUSION, HANGING DROP, temperature 293K | |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | VAPOR DIFFUSION, HANGING DROP, temperature 293K |