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