3OPY
Crystal structure of Pichia pastoris phosphofructokinase in the T-state
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.2 |
Synchrotron site | BESSY |
Beamline | 14.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-03-13 |
Detector | RAYONIX MX225HE |
Wavelength(s) | 0.918 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 161.658, 188.303, 231.560 |
Unit cell angles | 90.00, 92.85, 90.00 |
Refinement procedure
Resolution | 29.800 - 3.050 |
R-factor | 0.2019 |
Rwork | 0.200 |
R-free | 0.23180 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.240 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | BUSTER (2.8.0) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 29.800 |
High resolution limit [Å] | 3.050 |
Number of reflections | 262877 |
Completeness [%] | 53.2 |
Redundancy | 97.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 4.6 | 292 | 1 microliter of protein + 1 microliter of reservoir using streak seading, protein: 1mg/mL PFK, 10mM imidazol, 5mM mercaptoethanol, 10% glycerol, 10mM ATP, pH 7.0; reservoir: 0.7M ammonia sulfate, 0.1M sodium citrate pH 4.6, VAPOR DIFFUSION, temperature 292K |