5ETT
S. aureus 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.55 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 | 2015-04-28 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0329 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.546, 68.404, 53.125 |
| Unit cell angles | 90.00, 105.94, 90.00 |
Refinement procedure
| Resolution | 40.930 - 1.550 |
| R-factor | 0.15983 |
| Rwork | 0.158 |
| R-free | 0.19195 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5etq |
| RMSD bond length | 0.023 |
| RMSD bond angle | 2.208 |
| 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] | 40.930 | 1.580 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.099 | 0.856 |
| Number of reflections | 47134 | |
| <I/σ(I)> | 11.6 | 2.4 |
| Completeness [%] | 99.3 | 98.2 |
| Redundancy | 7.6 | 7.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.77 | 281 | Protein 6.9 mg/mL, 1 mM AMPCPP, 1 mM inhibitor, 0.182 MgCl2, 0.1 M tris chloride, 22%w/v PEG8000, 50 mM sodium thiocyanate |
