4P2V
Structure of the AI-2 processing enzyme LsrF in complex with the product of the LsrG reaction P-HPD
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-08-02 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.0750 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 78.617, 105.742, 170.402 |
Unit cell angles | 90.00, 101.43, 90.00 |
Refinement procedure
Resolution | 49.260 - 2.510 |
R-factor | 0.237 |
Rwork | 0.235 |
R-free | 0.27100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3gkf |
RMSD bond length | 0.007 |
RMSD bond angle | 1.371 |
Refinement software | PHENIX ((PHENIX.REFINE: DEV_1626)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.263 | 2.600 |
High resolution limit [Å] | 2.510 | 2.510 |
Rmerge | 0.104 | 0.491 |
Number of reflections | 92529 | |
<I/σ(I)> | 9.32 | 2.47 |
Completeness [%] | 99.0 | 97 |
Redundancy | 3.6 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 295 | 21% PEG 400, 110 mM MgCl2, 1 mM DTT, and 100 mM Tris pH 8.0 well solution. Drop was 1ul protein (7.3mg/ml) and 1 ul well solution. |