3SET

Ni-mediated Dimer of Maltose-binding Protein A216H/K220H by Synthetic Symmetrization (Form I)

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	72.940, 62.270, 89.710
Unit cell angles	90.00, 109.03, 90.00

Refinement procedure

Resolution	42.896 - 1.900
R-factor	0.234
Rwork	0.232
R-free	0.28220
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.004
RMSD bond angle	0.805
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]	42.896		1.950
High resolution limit [Å]	1.900	8.500	1.900
Rmerge	0.139	0.048	0.501
Number of reflections	60000	718	4416
<I/σ(I)>	7.11	13.17	2.67
Completeness [%]	99.6	97	99.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	290	0.1M TRIS, 25% (W/V) PEG 3350, pH 8.0, vapor diffusion, hanging drop, temperature 290K