8W0C
Crystal structure of Acetyl-CoA synthetase 2 from Candida albicans in complex with a cyclopentyl ester AMP 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 | 2023-11-23 |
Detector | DECTRIS EIGER2 XE 9M |
Wavelength(s) | 0.9786 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 139.409, 139.409, 543.793 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 49.580 - 2.350 |
R-factor | 0.1823 |
Rwork | 0.181 |
R-free | 0.20960 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.705 |
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] | 49.580 | 2.410 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.207 | 2.253 |
Rmeas | 0.212 | 2.310 |
Rpim | 0.047 | 0.508 |
Total number of observations | 2607480 | 195920 |
Number of reflections | 130936 | 9531 |
<I/σ(I)> | 12.6 | 1.7 |
Completeness [%] | 100.0 | |
Redundancy | 19.9 | 20.6 |
CC(1/2) | 0.998 | 0.786 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291 | Berkeley B12: 25% PEG 3350, 0.1M HEPES pH 7.5, 0.2M (NH4)2SO4. CaalA.00629.a.FS11.PD00399 at 20 mg/mL. 2mM HGN-1192 added to the protein prior to crystallization. Plate: plate 13750 well B12, drop 2. Puck: PSL-1715, Cryo: 20% Glycerol + 80% crystallant. |