1K62

Crystal Structure of the Human Argininosuccinate Lyase Q286R Mutant

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	298
Detector technology	IMAGE PLATE
Collection date	1999-10-15
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 31 2 1
Unit cell lengths	104.202, 104.202, 183.019
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	17.000 * - 2.650
R-factor	0.175
Rwork	0.175
R-free	0.23000 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1auw
RMSD bond length	0.006
RMSD bond angle	1.100
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	17.000	2.740
High resolution limit [Å]	2.650	2.650
Rmerge	0.100 *	0.460 *
Total number of observations	79294 *
Number of reflections	33242 *
<I/σ(I)>	8.1
Completeness [%]	97.8	99.2
Redundancy	2.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.1 *	298	Turner, M.A., (1997) Proc.Natl.Acad.Sci.USA, 94, 9063. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-15 (mg/ml)
2	1	drop	phosphate	50 (mM)
3	1	drop	dithiothreitol	5 (mM)
4	1	reservoir	phosphate	1.1 (M)