1LNS

Crystal Structure Analysis of the X-Prolyl Dipeptidyl Aminopeptidase From Lactococcus lactis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LURE BEAMLINE DW32
Synchrotron site	LURE
Beamline	DW32
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1998-03-26
Detector	MARRESEARCH
Wavelength(s)	0.9376
Spacegroup name	P 21 21 2
Unit cell lengths	92.500, 102.500, 101.500
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 2.200
Rwork	0.184
R-free	0.22300
Structure solution method	MIR
RMSD bond length	0.006
RMSD bond angle	24.400 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((AGROVATA)
Phasing software	MLPHARE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000 *	2.340
High resolution limit [Å]	2.200	2.200
Rmerge	0.057 *	0.170 *
Total number of observations	153738 *
Number of reflections	46073 *
Completeness [%]	95.8 *	95.3 *
Redundancy	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8 *	18 *	Chich, J.F., (1995) Proteins., 23. 278. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	Tris-HCl	50 (mM)	pH8.0
3	1	drop		0.1 (M)
4	1	drop	glycerol	10 (%)
5	1	reservoir	MES	50 (mM)	pH5.0
6	1	reservoir	PEG4000	7 (%)