1S18

Structure and protein design of human apyrase

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X25
Synchrotron site	NSLS
Beamline	X25
Temperature [K]	100
Detector technology	CCD
Collection date	2002-10-12
Detector	ADSC QUANTUM 4
Wavelength(s)	0.98, 0.9794, 0.9790, 0.9687
Spacegroup name	P 1
Unit cell lengths	43.163, 52.501, 77.925
Unit cell angles	99.44, 106.58, 99.89

Refinement procedure

Resolution	72.600 * - 1.700
R-factor	0.1591
Rwork	0.157
R-free	0.19100 *
Structure solution method	MAD
RMSD bond length	0.016
RMSD bond angle	1.500 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	72.600	1.760
High resolution limit [Å]	1.700	1.700
Rmerge	0.057	0.238
Number of reflections	65632
<I/σ(I)>	14.3	3.5
Completeness [%]	95.3 *	79.2
Redundancy	3.5	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	295	PEG MME 2000, sodium acetate, ammonium sulfate, strontium chloride, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG2000 MME	10-15 (%)
2	1	reservoir		100 (mM)	pH5.0
3	1	reservoir	ammonium sulfate	0.3-0.4 (M)
4	1	drop	protein	15 (mg/ml)