5ETK
E. coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.09 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 | 35.790, 57.690, 38.450 |
| Unit cell angles | 90.00, 115.57, 90.00 |
Refinement procedure
| Resolution | 34.680 - 1.090 |
| R-factor | 0.11672 |
| Rwork | 0.116 |
| R-free | 0.13640 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1q0n |
| RMSD bond length | 0.028 |
| RMSD bond angle | 1.983 |
| 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] | 34.680 | 1.110 |
| High resolution limit [Å] | 1.090 | 1.090 |
| Rmerge | 0.073 | 0.563 |
| Number of reflections | 57389 | |
| <I/σ(I)> | 14 | 3.1 |
| Completeness [%] | 97.7 | 95 |
| Redundancy | 7.2 | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.55 | 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, 0.16 M CaCl2 |
