1O86

Crystal Structure of Human Angiotensin Converting Enzyme in complex with lisinopril.

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	CCD
Collection date	2001-10-06
Detector	MARRESEARCH
Wavelength(s)	0.9537,1.2825,1.2832
Spacegroup name	P 21 21 21
Unit cell lengths	56.470, 84.900, 133.990
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	47.140 - 2.000
R-factor	0.18
Rwork	0.180
R-free	0.21880 *
Structure solution method	MAD
RMSD bond length	0.005 *
RMSD bond angle	1.200 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	CCP4
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.080
High resolution limit [Å]	2.000	2.010
Rmerge	0.058	0.238
Number of reflections	79319
<I/σ(I)>	11.6	2
Completeness [%]	95.9	72.1
Redundancy	2	1.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	4.7	16 *	PEG4000/SODIUM ACETATE., PH 4.70

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	HEPES	10 (mM)
2	1	drop	PMSF	0.1 (%)
3	1	reservoir	PEG4000	15 (%)
4	1	reservoir	sodium acetate trihydrate	50 (mM)	pH4.7
5	1	reservoir		10000 (nM)