5V0W
Crystal structure of glycylpeptide N-tetradecanoyltransferase from Plasmodium vivax in complex with inhibitor IMP-0001088
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2017-01-27 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97949 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 57.320, 119.130, 176.610 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.575 - 1.800 |
R-factor | 0.1473 |
Rwork | 0.147 |
R-free | 0.18400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4b14 |
RMSD bond length | 0.007 |
RMSD bond angle | 0.935 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.850 |
High resolution limit [Å] | 1.800 | 8.050 | 1.800 |
Rmerge | 0.107 | 0.036 | 0.515 |
Rmeas | 0.115 | 0.039 | 0.562 |
Number of reflections | 112736 | 1415 | 8213 |
<I/σ(I)> | 15.21 | 37.67 | 3.74 |
Completeness [%] | 99.9 | 99.4 | 99.4 |
Redundancy | 7.248 | 6.611 | 6.268 |
CC(1/2) | 0.998 | 0.999 | 0.905 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 290 | 27% PEG 3350, 200 mM Ammonium Sulfate, 100 mM BisTris pH 6.0, 0.5mM IMP-0001088, 0.5mM myristoyl CoA; protein conc 12.53mg/mL; hdg0-9 |