6BV1

Crystal structure of porcine aminopeptidase-N with Aspartic acid

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 24-ID-E
Synchrotron site	APS
Beamline	24-ID-E
Temperature [K]	100
Detector technology	CCD
Collection date	2012-06-29
Detector	ADSC QUANTUM 315
Wavelength(s)	1
Spacegroup name	C 1 2 1
Unit cell lengths	259.810, 62.682, 81.717
Unit cell angles	90.00, 100.40, 90.00

Refinement procedure

Resolution	50.000 - 2.000
R-factor	0.20973
Rwork	0.207
R-free	0.25270
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4fke
RMSD bond length	0.011
RMSD bond angle	1.132
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.070
High resolution limit [Å]	2.000	2.000
Number of reflections	85779
<I/σ(I)>	19.64	2.55
Completeness [%]	97.8	97.2
Redundancy	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.2	277	18% PEG3350, 200 MM LITHIUM SULFATE, 100 MM HEPES