3NH5

Crystal structure of E177A-mutant murine aminoacylase 3

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Detector technology	CCD
Collection date	2009-11-14
Detector	ADSC QUANTUM 315
Wavelength(s)	1.0000
Spacegroup name	P 62
Unit cell lengths	93.247, 93.247, 97.469
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	46.000 - 2.094
R-factor	0.1959
Rwork	0.194
R-free	0.22720
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Wild-type murine aminoacylase 3 to be deposited shortly.
RMSD bond length	0.008
RMSD bond angle	1.035
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	PHASER
Refinement software	PHENIX (1.5_2)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	46.000	50.000	2.180
High resolution limit [Å]	2.094	4.520	2.094
Rmerge	0.092	0.058	0.600
Number of reflections	27897
<I/σ(I)>	13.3
Completeness [%]	98.6	96.2	99.3
Redundancy	6.8	6.9	6.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5	293	2M Sodium formate, 0.1M Sodium acetate, pH5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K