5ETV
S. aureus 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.72 angstrom resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-06-09 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 61 |
| Unit cell lengths | 84.250, 84.250, 52.411 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 42.570 - 1.720 |
| R-factor | 0.18181 |
| Rwork | 0.181 |
| R-free | 0.20717 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4cwb |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.853 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.8.0103) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.570 | 1.750 |
| High resolution limit [Å] | 1.720 | 1.720 |
| Rmerge | 0.124 | 0.959 |
| Number of reflections | 22673 | |
| <I/σ(I)> | 20.3 | 5 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 20.2 | 20.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | Protein 6.9 mg/mL, 1 mM AMPCPP, 1 mM inhibitor, 2 mM magnesium chloride,0.186 M sodium nitrate, 18.4%w/v PEG3000, 50 mM sodium thiocyanate |
