2O57

Crystal Structure of a putative sarcosine dimethylglycine methyltransferase from Galdieria sulphuraria

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2006-11-08
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97923, 0.96400
Spacegroup name	C 2 2 21
Unit cell lengths	97.541, 291.433, 86.340
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.771 - 1.946
R-factor	0.168
Rwork	0.166
R-free	0.22100
Structure solution method	MAD
RMSD bond length	0.017
RMSD bond angle	1.452
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	48.771	2.020
High resolution limit [Å]	1.950	4.200	1.950
Rmerge	0.110	0.066	0.597
Number of reflections	89709
<I/σ(I)>	7.618		1.775
Completeness [%]	99.4	99.6	95
Redundancy	7.2	7.3	5.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	Protein Solution (10 MG/ML protein, 0.050 M sodium chloride, 0.0031 M sodium azide, 0.0003 M TCEP, 0.005 M Bis Tris pH 7.0) mixed in a 1:1 ratio with the Well Solution (23% MEPEG 5K, 0.03 M sarcosine, 0.1 M MOPS pH 7.0), Cryoprotected with: well solution supplemented with up to 15% glycerol, vapor diffusion, hanging drop, temperature 293K