2HPO

Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 8.2.2
Synchrotron site	ALS
Beamline	8.2.2
Temperature [K]	100
Detector technology	CCD
Collection date	2005-11-14
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9797, 0.9798, 0.9612
Spacegroup name	P 31 2 1
Unit cell lengths	120.438, 120.438, 170.561
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	19.940 - 1.650
R-factor	0.15781
Rwork	0.157
R-free	0.18062
Structure solution method	MAD
RMSD bond length	0.010
RMSD bond angle	1.171
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SHELXS
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.680
High resolution limit [Å]	1.650	1.650
Rmerge	0.520	0.500
Number of reflections	164250
<I/σ(I)>	14.1	2
Completeness [%]	95.5	89.2
Redundancy		2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	298	1.8 M Sodium Malonate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K