1QFX

PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM1A
Synchrotron site	ESRF
Beamline	BM1A
Temperature [K]	120
Detector technology	IMAGE PLATE
Collection date	1997-01-29
Detector	MARRESEARCH
Spacegroup name	P 61 2 2
Unit cell lengths	170.600, 170.600, 201.150
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	25.000 - 2.400
R-factor	0.18 *
Rwork	0.183
R-free	0.22500
Structure solution method	SIRAS
RMSD bond length	0.011
RMSD bond angle	1.600
Data reduction software	XDS
Data scaling software	XDS
Phasing software	SHELXS
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.500
High resolution limit [Å]	2.400	2.400
Rmerge	0.055 *	0.182 *
Total number of observations	173451 *
Number of reflections	58656
<I/σ(I)>	18.8	4.2
Completeness [%]	86.5	67.3
Redundancy	2.9	1.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7		0.1M HEPES/HCL PH 7.0, 2.4M AMMONIUM SULFATE

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	6 (mg/ml)
2	1	reservoir	ammonium sulfate	2.4 (M)
3	1	reservoir	HEPES	100 (mM)