1DMT

STRUCTURE OF HUMAN NEUTRAL ENDOPEPTIDASE COMPLEXED WITH PHOSPHORAMIDON

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	1999-06-20
Detector	MARRESEARCH
Spacegroup name	P 32 2 1
Unit cell lengths	107.580, 107.580, 112.840
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.100
R-factor	0.195
Rwork	0.195
R-free	0.24200
RMSD bond length	0.009
RMSD bond angle	1.480
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
High resolution limit [Å]	2.000
Rmerge	0.053 *	0.301 *
Total number of observations	189020 *
Number of reflections	49828 *
Completeness [%]	99.4 *	98.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.5	298	PEG 3350, AMMONIUM SULFATE, BIS TRIS, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	inhibitor	1 (mM)
3	1	reservoir	PEG3350	25 (%)
4	1	reservoir	ammonium sulfate	200 (mM)
5	1	reservoir	bis-Tris	100 (mM)