6BS6

SusG with mixed linkage amylosaccharide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2010-12-01
Detector	RAYONIX MX-300
Wavelength(s)	0.979
Spacegroup name	P 41
Unit cell lengths	127.439, 127.439, 129.410
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.400 - 2.170
R-factor	0.195
Rwork	0.194
R-free	0.23150
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3k8l
RMSD bond length	0.006
RMSD bond angle	1.000
Data reduction software	xia2
Data scaling software	xia2
Phasing software	PHENIX
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.400	2.248
High resolution limit [Å]	2.170	2.170
Rmerge	0.097	1.065
Rmeas	0.105	0.105
Number of reflections	701034	69620
<I/σ(I)>	8.89	1.4
Completeness [%]	99.7	99.31
Redundancy	6.4	6.4
CC(1/2)	0.996	0.795

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	Protein crystals of the SusG-D498N mutant were obtained via hanging drop vapor diffusion by mixing the protein (A280 = 15) with 10 mM alpha-D-glucosyl-maltotriosyl-maltotriose (O-GMH, Megazyme) against a crystallization liquor containing 18-20% PEG 4K, 100 mM HEPES pH 7.5, and 70 mM calcium acetate.