2HO4

Crystal Structure of Protein from Mouse Mm.236127

Experimental procedure

Experimental method	SINGLE WAVELENGTH
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	2006-06-18
Detector	MARMOSAIC 300 mm CCD
Spacegroup name	P 21 21 21
Unit cell lengths	46.586, 68.078, 190.982
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.500 - 2.200
R-factor	0.227
Rwork	0.224
R-free	0.28200
Structure solution method	SAD
RMSD bond length	0.020
RMSD bond angle	1.688
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.500	2.280
High resolution limit [Å]	2.200	2.200
Rmerge	0.079	0.350
Number of reflections	30718
<I/σ(I)>	13.469	3.344
Completeness [%]	96.1	73.4
Redundancy	12.9	7.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1			293	PROTEIN SOLUTION (10 MG/ML REDUCTIVELY METHYLATED PROTEIN, 0.050 M SODIUM CHLORIDE, 0.003 M SODIUM AZIDE, 0.0003 M TCEP, 0.005 BisTris PH 7.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (0.3 M NaH2PO4, 1.7 M K2HPO4) AND CRYOPROTECTED WITH FOMBLIN FOLLOWED BY PARATONE N, vapor diffusion, hanging drop, temperature 293K