2C2L

Crystal structure of the CHIP U-box E3 ubiquitin ligase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-1
Synchrotron site	ESRF
Beamline	ID23-1
Temperature [K]	100
Detector technology	CCD
Collection date	2005-03-17
Detector	MARRESEARCH
Spacegroup name	C 1 2 1
Unit cell lengths	76.042, 204.406, 144.709
Unit cell angles	90.00, 90.75, 90.00

Refinement procedure

Resolution	40.000 - 3.300
R-factor	0.2475
Rwork	0.247
R-free	0.28590
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	IN-HOUSE MODEL
RMSD bond length	0.010
RMSD bond angle	1.226
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	3.470
High resolution limit [Å]	3.300	3.300
Rmerge	0.070	0.330
Number of reflections	68272
<I/σ(I)>	10	2.7
Completeness [%]	98.1	98.1
Redundancy	2.1	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION	7.5	293	MCHIP WAS MIXED WITH HUMAN HSP90 C-TERMINAL PEPTIDE AT A 1:3 MOLAR RATIO, RESPECTIVELY, INCUBATED FOR 30 MIN AT 4C AND CONCENTRATED TO 10 MG/ML. INITIAL MULTIPLE CRYSTALS WERE GROWN BY VAPOUR DIFFUSION AT 20C AGAINST 30% W/V PEG4000, 100 MM TRIS [PH 7.5] AND 200 MM LITHIUM SULPHATE. SUBSEQUENT STREAK-SEEDING INTO SOLUTIONS OF 16% W/V PEG4000, 100 MM TRIS [PH 7.5] AND 400 MM LITHIUM SULPHATE PRODUCED SINGLE PLATES.