2NXF

Crystal Structure of a dimetal phosphatase from Danio rerio LOC 393393

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	62.584, 86.593, 157.315
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.276 - 1.700
R-factor	0.162
Rwork	0.161
R-free	0.18000
Structure solution method	MAD
RMSD bond length	0.011
RMSD bond angle	1.241
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]	48.276	80.000	1.740
High resolution limit [Å]	1.700	4.190	1.700
Rmerge	0.083	0.051	0.431
Number of reflections	47311
<I/σ(I)>	14.348		3.077
Completeness [%]	99.8	99.6	98.1
Redundancy	13.6	13.9	8.2

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 BisTris pH 7.0) mixed in a 1:1 ratio with the Well Solution (10.4% PEG 4K, 0.40 M sodium chloride, 0.10 M HEPES pH 7.5) Cryoprotected with: 15% PEG 8K, 0.30 M ammonium thiocyanate, 0.010 M sodium dihydrogen phosphate, 0.0005 M zinc sulfate, 0.10 M HEPPS pH 8.5 supplemented with up to 20% ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 293K