5G01
An unusual natural product primary sulfonamide: synthesis, carbonic anhydrase inhibition and protein x-ray structure of Psammaplin C
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 | CCD |
| Collection date | 2015-11-17 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 42.159, 41.494, 71.699 |
| Unit cell angles | 90.00, 104.26, 90.00 |
Refinement procedure
| Resolution | 69.490 - 1.400 |
| R-factor | 0.12977 |
| Rwork | 0.128 |
| R-free | 0.16534 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5a6h |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.718 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.500 | 1.420 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.070 | 0.740 |
| Number of reflections | 47179 | |
| <I/σ(I)> | 14.1 | 2.2 |
| Completeness [%] | 99.0 | 84.7 |
| Redundancy | 7.2 | 6.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 200 NL PLUS 200 NL OF PROTEIN AT 5 MGS/ML AND RESERVOIR IN SITTING DROP PLATES. RESERVOIR WAS 2.6 TO 2.8 M AMMONIUM SULFATE WITH 100 MM TRIS PH 8.5 |
