6HXJ
Structure of ATP citrate lyase from Chlorobium limicola in complex with citrate and coenzyme A.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID30B |
Synchrotron site | ESRF |
Beamline | ID30B |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-11-21 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.97625 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 101.670, 134.930, 177.710 |
Unit cell angles | 90.00, 101.65, 90.00 |
Refinement procedure
Resolution | 47.550 - 2.580 |
R-factor | 0.185 |
Rwork | 0.183 |
R-free | 0.21600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3PFF: Truncated human ATP citrate lyase |
RMSD bond length | 0.010 |
RMSD bond angle | 1.170 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | BUSTER (2.10.2) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.550 | 2.740 |
High resolution limit [Å] | 2.580 | 2.580 |
Rmeas | 0.111 | 1.765 |
Number of reflections | 144945 | 22149 |
<I/σ(I)> | 9.15 | 0.86 |
Completeness [%] | 98.5 | 93.5 |
Redundancy | 3.3 | 3.2 |
CC(1/2) | 0.997 | 0.361 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 8 | 293 | 24% PEG Smear High 0.1 M Tris pH 8.0 Protein sample buffer: 20 mM Citrate pH 6.0 150 mM NaCl 10 mM CoASH |