6M2C

Distinct mechanism of MUL1-RING domain simultaneously recruiting E2 enzyme and the substrate p53-TAD domain

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PAL/PLS BEAMLINE 7A (6B, 6C1)
Synchrotron site	PAL/PLS
Beamline	7A (6B, 6C1)
Temperature [K]	93
Detector technology	CCD
Collection date	2016-05-04
Detector	ADSC QUANTUM 270
Wavelength(s)	0.9793
Spacegroup name	P 1 21 1
Unit cell lengths	47.207, 141.241, 68.047
Unit cell angles	90.00, 104.81, 90.00

Refinement procedure

Resolution	45.639 - 2.702
R-factor	0.2159
Rwork	0.212
R-free	0.25830
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3t6p 2esk
RMSD bond length	0.006
RMSD bond angle	1.292
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.800
High resolution limit [Å]	2.700	5.810	2.700
Rmerge	0.085	0.054	0.287
Rmeas	0.093	0.059	0.337
Rpim	0.038	0.022	0.171
Total number of observations	107188
Number of reflections	21200	2388	1768
<I/σ(I)>	13.2
Completeness [%]	89.9	99.3	74.8
Redundancy	5.1	6.9	3
CC(1/2)		0.998	0.618

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6	291	4% v/v Tacsimate pH 6.0, 12% w/v Polyethylene glycol 3350