5G0B
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 | 41.706, 41.286, 72.130 |
Unit cell angles | 90.00, 104.19, 90.00 |
Refinement procedure
Resolution | 69.930 - 1.550 |
R-factor | 0.13473 |
Rwork | 0.132 |
R-free | 0.17851 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5a6h |
RMSD bond length | 0.011 |
RMSD bond angle | 1.658 |
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] | 41.300 | 1.580 |
High resolution limit [Å] | 1.550 | 1.550 |
Rmerge | 0.080 | 0.720 |
Number of reflections | 34094 | |
<I/σ(I)> | 15.8 | 2.6 |
Completeness [%] | 98.0 | 95.7 |
Redundancy | 7.5 | 7.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | SITTING DROPS WITH 150 NL PROTEIN AT 5.5 MG/ML WITH 120 NL RESERVOIR AND 30 NL SEEDS. THE RESERVOIR HAD 2.6 TO 2.8 M AMMONIUM SULFATE WITH 100 MM TRIS PH 8.5 |