7M26
Human carbonic anhydrase II in complex with pioglitazone
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-09-14 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.953656 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.379, 41.437, 72.069 |
Unit cell angles | 90.00, 104.38, 90.00 |
Refinement procedure
Resolution | 35.658 - 1.300 |
Rwork | 0.119 |
R-free | 0.14540 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6odz |
RMSD bond length | 0.011 |
RMSD bond angle | 1.708 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.440 | 1.320 |
High resolution limit [Å] | 1.300 | 1.300 |
Rmerge | 0.062 | 0.479 |
Rpim | 0.039 | 0.320 |
Number of reflections | 59758 | 2962 |
<I/σ(I)> | 14.8 | |
Completeness [%] | 99.9 | |
Redundancy | 6.7 | |
CC(1/2) | 0.999 | 0.862 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.3 | 293 | Protein concentration was 4 mg/mL; equal volumes (250 nL) of protein plus reservoir were added to the plate; the reservoir was 1.5 M tri-potassium citrate, 0.1 M tris buffer at pH 8.3. |