3SES

Cu-mediated Dimer of Maltose-binding Protein A216H/K220H by Synthetic Symmetrization

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-C
Synchrotron site	APS
Beamline	24-ID-C
Temperature [K]	100
Detector technology	CCD
Collection date	2010-10-16
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9792
Spacegroup name	P 1 21 1
Unit cell lengths	72.850, 61.250, 89.450
Unit cell angles	90.00, 109.71, 90.00

Refinement procedure

Resolution	64.978 - 1.900
R-factor	0.1733
Rwork	0.172
R-free	0.20510
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	0.952
Data scaling software	XSCALE
Phasing software	PHASER (2.1.4)
Refinement software	PHENIX (1.6.4_486)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	64.978		1.950
High resolution limit [Å]	1.900	8.500	1.900
Rmerge	0.062	0.017	0.532
Number of reflections	57840	686	4203
<I/σ(I)>	15.54	46.46	2.38
Completeness [%]	98.5	96.1	97.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	290	0.1M TRIS, 0.2M MAGNESIUM CHLORIDE, 20% (W/V) PEG 8000, pH 8.0, vapor diffusion, hanging drop, temperature 290K