1ND6

Crystal Structures of Human Prostatic Acid Phosphatase in Complex with a Phosphate Ion and alpha-Benzylaminobenzylphosphonic Acid Update the Mechanistic Picture and Offer New Insights into Inhibitor Design

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1997-12-01
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	119.890, 203.320, 70.890
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 * - 2.420 *
R-factor	0.1981
Rwork	0.198
R-free	0.25200 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	22.400 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.470
High resolution limit [Å]	2.400 *	2.360
Rmerge	0.056 *
Number of reflections	89003
Completeness [%]	99.5	99.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	10	298	PEG, KCL, Glycine, pH 10.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	7-10 (mg/ml)
2	1	1	PEG1500	30 (%)
3	1	1	PEG1000	7 (%)
4	1	1	PEG400	6 (%)
5	1	1		100 (mM)
6	1	1	glycine	100 (mM)	pH10.0