1I40

STRUCTURE OF INORGANIC PYROPHOSPHATASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-06-21
Detector	MAR scanner 345 mm plate
Wavelength(s)	0.906
Spacegroup name	H 3 2
Unit cell lengths	109.520, 109.520, 75.080
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	12.000 - 1.100
R-factor	0.117
Rwork	0.117
R-free	0.15300
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.018 *
RMSD bond angle	0.038 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHELXL-97
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.060
High resolution limit [Å]	1.100 *	1.100 *
Rmerge	0.034	0.350 *
Total number of observations	662283 *
Number of reflections	79833
<I/σ(I)>	15.9	2.6
Completeness [%]	99.6	99.7 *
Redundancy	8.3	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	298	pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5-8 (mg/ml)
2	1	drop		1 (M)
3	1	drop		180 (mM)
4	1	drop	sodium acetate	0.2 (M)	pH5.0
5	1	reservoir		1.4-2.0 (M)
6	1	reservoir		180 (mM)
7	1	reservoir	sodium acetate	0.2 (M)	pH5.0