5N4W

Crystal structure of the Cul2-Rbx1-EloBC-VHL ubiquitin ligase complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04-1
Synchrotron site	Diamond
Beamline	I04-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-08-01
Detector	DECTRIS PILATUS 6M-F
Wavelength(s)	0.928
Spacegroup name	C 2 2 21
Unit cell lengths	86.038, 190.962, 238.885
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	95.480 - 3.900
R-factor	0.304
Rwork	0.302
R-free	0.34600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	HOMOLOGY MODEL
RMSD bond length	0.003
RMSD bond angle	0.692
Data reduction software	DIALS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX ((1.11_2558: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	95.481	4.270
High resolution limit [Å]	3.900	3.900
Rmerge	0.114	0.732
Number of reflections	34407
<I/σ(I)>	10.2	2.2
Completeness [%]	100.0	100
Redundancy	5.7	5.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.6	293	0.1 M Tris pH 7.6, 0.15 M ammonium sulphate, 15% polyethyleneglycol 4000 and 3% 1,4-dioxane or 4% acetonitrile. The sample was crystallised in the presence of a 19-mer peptide mimicking the substrate HIF-1alpha - residues 559-577 (DEALAPYIPMDDDFQLRSF, with the mutations L559D and M561A and P564 is hydroxyproline).