4GSW

Crystal structure of ubiquitin from Entamoeba histolytica to 2.15 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
Wavelength(s)	1.000
Spacegroup name	P 21 21 21
Unit cell lengths	38.631, 49.865, 76.824
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	34.513 - 2.150
R-factor	0.1994
Rwork	0.193
R-free	0.25610
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ubq
RMSD bond length	0.014
RMSD bond angle	1.493
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]	40.000	2.170
High resolution limit [Å]	2.150	2.150
Rmerge	0.085	0.279
Number of reflections	8430
<I/σ(I)>	13.6	3.1
Completeness [%]	98.1	96.8
Redundancy	3.5	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	291	EhUbiquitin at 13 mg/mL in S200 buffer was mixed 1:1 with and equilibrated against crystallization solution containing 22% (w/v) PEG 3350, 200 mM LiSO4, and 100 mM Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K