7M23
Human carbonic anhydrase II in complex with troglitazone
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 | 42.333, 41.292, 71.688 |
Unit cell angles | 90.00, 104.36, 90.00 |
Refinement procedure
Resolution | 39.943 - 1.300 |
Rwork | 0.120 |
R-free | 0.15100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6odz |
RMSD bond length | 0.011 |
RMSD bond angle | 1.608 |
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] | 41.290 | 1.320 |
High resolution limit [Å] | 1.300 | 1.300 |
Rmerge | 0.071 | 0.627 |
Rpim | 0.045 | 0.416 |
Number of reflections | 58740 | 2886 |
<I/σ(I)> | 12.2 | |
Completeness [%] | 99.1 | |
Redundancy | 6.6 | |
CC(1/2) | 0.998 | 0.825 |
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. |