5ETS
S. aureus 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.95 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 | 47.790, 68.580, 52.990 |
| Unit cell angles | 90.00, 105.94, 90.00 |
Refinement procedure
| Resolution | 40.900 - 1.950 |
| R-factor | 0.19046 |
| Rwork | 0.189 |
| R-free | 0.21815 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5etq |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.747 |
| 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] | 40.900 | 2.000 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.149 | 0.758 |
| Number of reflections | 24055 | |
| <I/σ(I)> | 10 | 2.9 |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 7 | 7.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.1 | 281 | Protein 6.9 mg/mL 1 mM AMPCPP, 1 mM inhibitor, 0.182 MgCl2, 0.1 M tris chloride, 17.2%w/v PEG8000, 50 mM sodium thiocyanate |
