4GU2

Crystal structure of ubiquitin from Entamoeba histolytica to 1.35 Angstrom

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	2012-04-08
Detector	MAR scanner 300 mm plate
Spacegroup name	P 32 2 1
Unit cell lengths	49.798, 49.798, 63.830
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	25.650 - 1.350
R-factor	0.215
Rwork	0.212
R-free	0.26920
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ubq
RMSD bond length	0.015
RMSD bond angle	1.642
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHENIX (AutoMR)
Refinement software	PHENIX ((phenix.refine: 1.8_1069))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.654	1.360
High resolution limit [Å]	1.350	1.350
Rmerge	0.043	0.557
Number of reflections	20493
<I/σ(I)>	100	6.9
Completeness [%]	99.3	100
Redundancy	19.2	17.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	3.5	291	EhUbiquitin at 17 mg/mL was mixed 1:1 with and equilibrated against crystallization solution containing 25% (w/v) PEG 3350 and 100 mM citric acid, pH 3.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K