4UMC
Structural analysis of substrate-mimicking inhibitors in complex with Neisseria meningitidis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase - the importance of accommodating the active site water
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX1 |
Synchrotron site | Australian Synchrotron |
Beamline | MX1 |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2013-07-06 |
Detector | ADSC CCD |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 73.421, 137.013, 76.476 |
Unit cell angles | 90.00, 96.48, 90.00 |
Refinement procedure
Resolution | 75.990 - 2.340 |
R-factor | 0.20397 |
Rwork | 0.203 |
R-free | 0.23038 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4hsn |
RMSD bond length | 0.012 |
RMSD bond angle | 1.459 |
Data reduction software | iMOSFLM |
Phasing software | CCP4 |
Refinement software | REFMAC (5.8.0049) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.880 | 2.400 |
High resolution limit [Å] | 2.340 | 2.340 |
Rmerge | 0.150 | |
Number of reflections | 63250 | |
<I/σ(I)> | 8 | 1.1 |
Completeness [%] | 99.9 | 99.8 |
Redundancy | 3.8 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.3 | pH 7.3 |