2I3C

Crystal Structure of an Aspartoacylase from Homo Sapiens

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 22-ID
Synchrotron site	APS
Beamline	22-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2006-08-05
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97926
Spacegroup name	P 42 21 2
Unit cell lengths	145.551, 145.551, 103.396
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	48.716 - 2.800
R-factor	0.197
Rwork	0.195
R-free	0.24300
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2gu2
RMSD bond length	0.016
RMSD bond angle	1.551
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.716	48.716	2.900
High resolution limit [Å]	2.800	6.030	2.800
Rmerge	0.164	0.087	0.582
Number of reflections	27367
<I/σ(I)>	10.612		1.866
Completeness [%]	97.9	99.8	81.4
Redundancy	13.3	14.2	6.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		277	PROTEIN SOLUTION (10 MG/ML PROTEIN, 0.050 M SODIUM CHLORIDE, 0.0003 M TCEP, 0.005 M Tris PH 8.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (1.344 M K2HPO4, 0.056 M NaH2PO4) CRYOPROTECTED WITH WELL SOLUTION WITH 25% Ethylene glycol, vapor diffusion, hanging drop, temperature 277K
1	VAPOR DIFFUSION, HANGING DROP		277	PROTEIN SOLUTION (10 MG/ML PROTEIN, 0.050 M SODIUM CHLORIDE, 0.0003 M TCEP, 0.005 M Tris PH 8.0) MIXED IN A 1:1 RATIO WITH THE WELL SOLUTION (1.344 M K2HPO4, 0.056 M NaH2PO4) CRYOPROTECTED WITH WELL SOLUTION WITH 25% Ethylene glycol, vapor diffusion, hanging drop, temperature 277K