4DVG
Crystal structure of E. histolytica Formin1 bound to EhRho1-GTPgammaS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2011-11-22 |
Detector | MAR scanner 300 mm plate |
Wavelength(s) | 0.9795 |
Spacegroup name | P 61 |
Unit cell lengths | 138.564, 138.564, 57.765 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 35.673 - 2.604 |
R-factor | 0.2188 |
Rwork | 0.215 |
R-free | 0.25120 |
Structure solution method | SAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.233 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX (AutoSol) |
Refinement software | PHENIX ((phenix.refine: 1.7.1_743)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.630 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.085 | 0.580 |
Number of reflections | 19500 | |
<I/σ(I)> | 2.1 | |
Completeness [%] | 98.4 | |
Redundancy | 9.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | EhRho1-GTPgammaS at 5 mg/mL and and EhFormin1 at 10 mg/mL were mixed in crystallization buffer (50 mM Tris pH 8.0, 250 mM NaCl, 2.5% (v/v) glycerol, 5 mM DTT, 50 microM GTPgammaS, 1 mM magnesium chloride) and allowed to form a complex for 30 minutes at room temperature. The protein solution was then mixed 1:1 and equilibrated against crystallization solution (18% PEG 3350, 100 mM Tris pH 8.5, 200 mM magnesium chloride)., VAPOR DIFFUSION, HANGING DROP, temperature 293K |