4MIT
Crystal structure of E. histolytica RacC bound to the EhPAK4 PBD
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 | 2013-02-14 |
Detector | MAR scanner 300 mm plate |
Wavelength(s) | 1.000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.322, 211.957, 49.780 |
Unit cell angles | 90.00, 102.85, 90.00 |
Refinement procedure
Resolution | 46.896 - 2.350 |
R-factor | 0.1785 |
Rwork | 0.176 |
R-free | 0.22000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3th5 |
RMSD bond length | 0.013 |
RMSD bond angle | 1.277 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8.1_1168)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.900 | 2.370 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.067 | 0.687 |
Number of reflections | 36818 | |
<I/σ(I)> | 34.7 | 2.8 |
Completeness [%] | 89.0 | 85 |
Redundancy | 5 | 5.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | EhRacC-GTP/EhPAK4 PBD complex was mixed 1:1 with and equilibrated against crystallization solution containing 22% (w/v) PEG 4000, 200 mM magnesium chloride, and 100 mM MES, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |