5ETM
E. coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.46 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 | 2015-09-26 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 35.763, 57.631, 38.407 |
| Unit cell angles | 90.00, 115.49, 90.00 |
Refinement procedure
| Resolution | 34.670 - 1.460 |
| R-factor | 0.2063 |
| Rwork | 0.204 |
| R-free | 0.23939 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5etk |
| RMSD bond length | 0.021 |
| RMSD bond angle | 2.206 |
| 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] | 34.670 | 1.480 |
| High resolution limit [Å] | 1.460 | 1.460 |
| Rmerge | 0.097 | 0.662 |
| Number of reflections | 24472 | |
| <I/σ(I)> | 11.6 | 2.7 |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 7.1 | 6.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.55 | 293 | Protein 6.6 mg/mL, 1 mM AMPCPP, 1 mM inhibitor, 2 mM Magnesium Chloride, 27.5 %w/v PEG4000, 0.1 M sodium HEPES, 0.196 M Calcium Chloride |
