5A6H
Synthesis, carbonic anhydrase inhibition and protein X-ray structure of the unusual natural product primary sulfonamide Psammaplin C
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-06-02 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.300, 41.385, 72.460 |
| Unit cell angles | 90.00, 104.66, 90.00 |
Refinement procedure
| Resolution | 70.100 - 1.570 |
| R-factor | 0.14768 |
| Rwork | 0.145 |
| R-free | 0.19320 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4cq0 |
| RMSD bond length | 0.020 |
| RMSD bond angle | 2.069 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0123) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.400 | 1.600 |
| High resolution limit [Å] | 1.570 | 1.570 |
| Rmerge | 0.080 | 0.680 |
| Number of reflections | 33092 | |
| <I/σ(I)> | 16.5 | 2.8 |
| Completeness [%] | 98.0 | 95.6 |
| Redundancy | 7.5 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 8 | 281 | EQUAL VOLUMES OF PROTEIN AND RESERVOIR (250 NL EACH) AT 8C WITH THE PROTEIN AT 7.5 MG/ML AND THE RESERVOIR BEING 2.6 M AMMONIUM SULFATE, 100 MM TRIS PH 8 |
