1Y7E

The Crystal Structure of Aminopeptidase I from Borrelia burgdorferi B31

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X29A
Synchrotron site	NSLS
Beamline	X29A
Temperature [K]	100
Detector technology	CCD
Collection date	2004-11-04
Detector	ADSC QUANTAM Q315
Wavelength(s)	0.98
Spacegroup name	F 4 3 2
Unit cell lengths	244.271, 244.271, 244.271
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.810 - 3.200
R-factor	0.202
Rwork	0.202
R-free	0.25800
Structure solution method	SAD
RMSD bond length	0.007
RMSD bond angle	1.600
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.310
High resolution limit [Å]	3.200	3.200
Rmerge	0.094	0.233
Number of reflections	32224
Completeness [%]		100
Redundancy	7.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	10% PEG 4k, 0.1M Bis-tris, 0.2M MgCl2, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K