5ETO
E. coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.07 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 | 2015-04-14 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 35.770, 57.750, 38.420 |
| Unit cell angles | 90.00, 115.46, 90.00 |
Refinement procedure
| Resolution | 34.690 - 1.070 |
| R-factor | 0.12994 |
| Rwork | 0.129 |
| R-free | 0.14996 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5etk |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.968 |
| 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] | 34.690 | 1.090 |
| High resolution limit [Å] | 1.070 | 1.070 |
| Rmerge | 0.097 | 0.819 |
| Number of reflections | 61436 | |
| <I/σ(I)> | 10.1 | 2 |
| Completeness [%] | 98.6 | 96.8 |
| Redundancy | 7.1 | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.88 | 293 | PROTEIN 6.6 MG/ML 1 MM AMPCPP, 1 MM INHIBITOR, 2 MM MAGNESIUM CHLORIDE, 22%w/v PEG4000, 0.1 M SODIUM HEPES, 0.22 M CACL2 |
