5ETP
E. coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.05 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 | 35.950, 57.770, 38.640 |
| Unit cell angles | 90.00, 116.11, 90.00 |
Refinement procedure
| Resolution | 34.700 - 1.050 |
| R-factor | 0.10791 |
| Rwork | 0.107 |
| R-free | 0.12504 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1q0n |
| RMSD bond length | 0.019 |
| RMSD bond angle | 2.099 |
| 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] | 34.700 | 1.060 |
| High resolution limit [Å] | 1.050 | 1.050 |
| Rmerge | 0.087 | 0.298 |
| Number of reflections | 66451 | |
| <I/σ(I)> | 13.4 | 5.1 |
| Completeness [%] | 99.8 | 99.2 |
| Redundancy | 7.1 | 6.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9.1 | 281 | PROTEIN 6.6 MG/ML 1 MM AMPCPP, 1 MM INHIBITOR, 2 MM MAGNESIUM CHLORIDE, 20%w/v PEG4000, 0.1 M TRIS CHLORIDE, 0.172 M CALCIUM CHLORIDE |
