7RBX
Crystal structure of isocitrate lyase and phosphorylmutase:isocitrate lyase from Brucella melitensis biovar Abortus 2308 bound to itaconic acid
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2021-06-10 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97872 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 76.750, 136.270, 181.980 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 47.590 - 1.800 |
R-factor | 0.143 |
Rwork | 0.143 |
R-free | 0.16630 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3eol |
RMSD bond length | 0.006 |
RMSD bond angle | 0.781 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX (dev-4274) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 47.590 | 47.590 | 1.850 |
High resolution limit [Å] | 1.800 | 8.050 | 1.800 |
Rmerge | 0.072 | 0.040 | 0.539 |
Rmeas | 0.078 | 0.043 | 0.581 |
Total number of observations | 1200309 | ||
Number of reflections | 175674 | 2171 | 12899 |
<I/σ(I)> | 14.83 | 33.24 | 3.36 |
Completeness [%] | 99.4 | 98.5 | 99.6 |
Redundancy | 6.833 | 6.565 | 7.05 |
CC(1/2) | 0.998 | 0.998 | 0.923 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 287 | BrabA.00014.a.A1.PW38950 at 25.5 mg/mL with 2.5 mM itaconic acid and 2.5 mM MgCl2 against MCSG1 screen condition G8: 0.2 M ammonium sulfate, 0.1 M Tris pH 8.5, 25% PEG 3350 supplemented with 20% ethylene glycol as cryo-protectant; crystal tracking ID 321126g8, unique puck ID qrt6-6 |