2GU2

Crystal Structure of an Aspartoacylase from Rattus norvegicus

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-D
Synchrotron site	APS
Beamline	23-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2006-04-19
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97928, 0.95373
Spacegroup name	C 1 2 1
Unit cell lengths	92.581, 135.778, 54.033
Unit cell angles	90.00, 101.49, 90.00

Refinement procedure

Resolution	41.750 - 1.805
Rwork	0.149
R-free	0.19400
Structure solution method	MAD
RMSD bond length	0.020
RMSD bond angle	1.616
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	80.000	80.000	1.840
High resolution limit [Å]	1.800	4.440	1.800
Rmerge	0.093	0.060	0.470
Number of reflections	58208
<I/σ(I)>	9.949		2.167
Completeness [%]	97.5	99.7	86.6
Redundancy	7.1	7.5	4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293	PROTEIN SOLUTION (10 MG/ML PROTEIN, 0.050 M SODIUM CHLORIDE, 0.003 M SODIUM AZIDE, 0.0003 M TCEP, 0.005 MES PH 7.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (1.9 M Ammonium sulfate, 0.10 M HEPPS PH 8.5). Crystal cryo-protected with well solution supplemented with a final concentration of 30% Ethylene glycol, temperature 293K, VAPOR DIFFUSION, HANGING DROP