6ZM3

The structure of an E2 ubiquitin-conjugating complex (UBC2-UEV1) essential for Leishmania amastigote differentiation

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	100
Detector technology	PIXEL
Collection date	2019-04-08
Detector	DECTRIS EIGER2 XE 16M
Wavelength(s)	0.976254
Spacegroup name	P 1 21 1
Unit cell lengths	32.523, 72.568, 120.094
Unit cell angles	90.00, 91.84, 90.00

Refinement procedure

Resolution	46.250 - 1.700
Rwork	0.223
R-free	0.26030
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB ID: 1J7D
RMSD bond length	0.007
RMSD bond angle	1.564
Data reduction software	Aimless (0.7.4)
Data scaling software	Aimless (0.7.4)
Phasing software	MOLREP (11.7.02)
Refinement software	REFMAC (5.8.0258)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.250	46.250	1.730
High resolution limit [Å]	1.650	9.040	1.700
Rmerge	0.092	0.047	1.449
Rmeas	0.120	0.061	1.635
Rpim	0.075	0.038	0.747
Number of reflections	67149	446	3267
<I/σ(I)>	6.7
Completeness [%]	100.0
Redundancy	4.2	4.2	4.2
CC(1/2)	0.996	0.997	0.368

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	298	UBC2 and UEV1 were mixed in a 1:1 molar ratio to a final concentration of 6.6 mg mL-1 and incubated on ice for 30 min. Crystals were grown using a sitting drop method with a 1:1 ratio of protein to reservoir solution (0.1 M Bis-Tris propane, pH 7.5, 0.2 M sodium formate and 20% PEG) in the drop. Crystals took 2 days to appear.