5ETN
E. coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.40 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 | 35.880, 57.890, 38.610 |
| Unit cell angles | 90.00, 115.12, 90.00 |
Refinement procedure
| Resolution | 34.960 - 1.400 |
| R-factor | 0.18421 |
| Rwork | 0.182 |
| R-free | 0.21898 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5etk |
| RMSD bond length | 0.041 |
| RMSD bond angle | 2.503 |
| 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] | 34.960 | 1.420 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.111 | 0.678 |
| Number of reflections | 28184 | |
| <I/σ(I)> | 9.3 | 2.6 |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 7 | 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, 0.22 M calcium chloride |
