3SE6

Crystal structure of the human Endoplasmic Reticulum Aminopeptidase 2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X13
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X13
Temperature [K]	100
Detector technology	CCD
Collection date	2011-03-15
Detector	MAR CCD 165 mm
Wavelength(s)	0.81230
Spacegroup name	P 1 21 1
Unit cell lengths	74.579, 134.362, 128.009
Unit cell angles	90.00, 90.71, 90.00

Refinement procedure

Resolution	10.997 - 3.080
R-factor	0.2155
Rwork	0.212
R-free	0.27700
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	1.199
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	PHENIX ((phenix.refine))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.900	3.100
High resolution limit [Å]	2.990	2.990
Number of reflections	50371
Completeness [%]	98.6	97.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	277	10% PEG 8000, 20% ethylene glycol, 61 mM MES, 39 mM imidazole, 20 mM sodium-L-glutamate, 20 mM D-L-alanine, 20 mM glycine, 20 mM D-L-lysine, 20 mM D-L-serine, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K