4GPR

Crystal structure of EhUbc5, a ubiquitin conjugating enzyme from Entamoeba histolytica

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-BM
Synchrotron site	APS
Beamline	22-BM
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2012-07-16
Detector	MAR scanner 300 mm plate
Wavelength(s)	1.000
Spacegroup name	P 21 21 21
Unit cell lengths	46.973, 49.577, 63.464
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.069 - 1.600
R-factor	0.1737
Rwork	0.171
R-free	0.20220
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2cp4
RMSD bond length	0.014
RMSD bond angle	1.504
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]	50.000	1.610
High resolution limit [Å]	1.600	1.600
Rmerge	0.044	0.309
Number of reflections	19998
<I/σ(I)>	45.6	2.8
Completeness [%]	99.3	87.3
Redundancy	8.2	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	291	EhUbc5 at 8 mg/mL concentration in buffer containing 50 mM HEPES and 100 mM NaCl was mixed 1:1 and equilibrated against crystallization solution (100 mM Tris, 14% (w/v) polyvinylpyrrolidone K 15, and 0.5 mM cobalt (II) chloride), pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K