5ETQ
S. aureus 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.96 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 | 2015-02-07 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9707 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.630, 68.200, 52.820 |
| Unit cell angles | 90.00, 106.05, 90.00 |
Refinement procedure
| Resolution | 50.760 - 1.960 |
| R-factor | 0.18384 |
| Rwork | 0.182 |
| R-free | 0.21566 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4cwb |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.884 |
| 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] | 68.200 | 2.010 |
| High resolution limit [Å] | 1.960 | 1.960 |
| Rmerge | 0.117 | 0.497 |
| Number of reflections | 23517 | |
| <I/σ(I)> | 9.1 | 3.2 |
| Completeness [%] | 100.0 | 99.8 |
| Redundancy | 7 | 6.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 281 | PROTEIN 6.9 MG/ML, 1 MM AMPCPP, 1 MM INHIBITOR, 0.202 M MAGNESIUM CHLORIDE, 0.1 M TRIS CHLORIDE, 20%w/v PEG8000, 50 MM SODIUM THIOCYANATE |
