1B65

Structure of l-aminopeptidase d-ala-esterase/amidase from ochrobactrum anthropi, a prototype for the serine aminopeptidases, reveals a new variant among the ntn hydrolase fold

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LURE BEAMLINE DW32
Synchrotron site	LURE
Beamline	DW32
Temperature [K]	294
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	P 21 21 2
Unit cell lengths	156.970, 96.220, 154.410
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	12.500 - 1.820
R-factor	0.169 *
Rwork	0.169
R-free	0.20600
Structure solution method	MIR
RMSD bond length	0.013
RMSD bond angle	0.034
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CCP4
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	12.500
High resolution limit [Å]	1.820	1.820 *
Rmerge	0.081 *	0.288 *
Total number of observations	473750 *
Number of reflections	56600
Completeness [%]	95.8	91.9 *
Redundancy	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	9	294 *	pH 9.0

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir	PEG2000 MME	13-16 (%(w/v))
3	1	reservoir	bicine	100 (mM)
4	1	reservoir		1 (M)