4R8L

Crystal structure of the Asp-bound guinea pig L-asparaginase 1 catalytic domain

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2013-07-31
Detector	MARMOSAIC 300 mm CCD
Spacegroup name	I 2 2 2
Unit cell lengths	123.210, 156.000, 158.820
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.961 - 2.410
R-factor	0.20727
Rwork	0.206
R-free	0.23612
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.368
Data reduction software	XDS
Data scaling software	XDS
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0071)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	111.290	2.550
High resolution limit [Å]	2.410	2.410
Number of reflections	58821
Completeness [%]	98.7	96.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	293	0.1 M HEPES, 15% PEG 4000, 10 mM L-aspartic acid sodium salt monohydrate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K