8W0M
Crystal structure of Acetyl-CoA synthetase 2 from Candida albicans in complex with a Acetyl Sulfamate AMP ester inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 19-ID |
Synchrotron site | NSLS-II |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2023-12-09 |
Detector | DECTRIS EIGER2 XE 9M |
Wavelength(s) | 0.9785 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 101.399, 115.398, 106.265 |
Unit cell angles | 90.00, 116.40, 90.00 |
Refinement procedure
Resolution | 47.590 - 3.100 |
R-factor | 0.19 |
Rwork | 0.188 |
R-free | 0.22950 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.002 |
RMSD bond angle | 0.520 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((dev_5233: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.410 | 3.180 |
High resolution limit [Å] | 3.100 | 3.100 |
Rmerge | 0.165 | 1.440 |
Rmeas | 0.179 | 1.565 |
Rpim | 0.067 | 0.607 |
Total number of observations | 279234 | 19321 |
Number of reflections | 39912 | 2931 |
<I/σ(I)> | 9.2 | 1.4 |
Completeness [%] | 99.9 | |
Redundancy | 7 | 6.6 |
CC(1/2) | 0.995 | 0.570 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 291 | Berkeley B11: 100 mM Tris pH 8.5, 200 mM Ammonium sulfate, 25% (w/v) PEG 3350. CaalA.00629.a.FS11.PD00399 at 20 mg/mL. 2mM HGN-1076 added to the protein prior to crystallization. Plate: plate 13749 well C11 drop 1. Puck: PSL-1115, Cryo: 20% PEG 200 + 80% crystallant. |