1ND7

Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain E3 Ligase

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM30A
Synchrotron site	ESRF
Beamline	BM30A
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-10-01
Detector	MARRESEARCH
Wavelength(s)	0.979, 0.980, 0.972
Spacegroup name	P 1
Unit cell lengths	45.200, 50.850, 58.430
Unit cell angles	113.47, 99.21, 102.26

Refinement procedure

Resolution	32.080 - 2.100
Rwork	0.243
R-free	0.27700 *
Structure solution method	MAD
RMSD bond length	0.016
RMSD bond angle	21.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	32.000 *
High resolution limit [Å]	2.200 *
Rmerge	0.033 *	0.324 *
Number of reflections	21708
Completeness [%]	97.0 *	99 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.5	4 *	ammonium acetate, beta-mercaptoethanol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	succinic acid	100 (mM)	pH5.5
3	1	reservoir	ammonium acetate	0.75-1.0 (M)
4	1	reservoir	beta-mercaptoethanol	20 (mM)