1LOO

Crystal Structure of the Mouse-Muscle Adenylosuccinate Synthetase Ligated with GTP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-03-19
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 43 21 2
Unit cell lengths	69.935, 69.935, 198.090
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 2.200
Rwork	0.244
R-free	0.27600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1j4b
RMSD bond length	0.006
RMSD bond angle	1.200 *
Phasing software	AMoRE
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	65.900	2.280
High resolution limit [Å]	2.200	2.200
Rmerge	0.081 *	0.312 *
Total number of observations	126081 *
Number of reflections	25715 *
<I/σ(I)>	20	2.3
Completeness [%]	89.5 *	98.5 *
Redundancy	4.9	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	296	PEG 8000, magnesium acetate, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 296K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	enzyme	10 (mg/ml)
2	1	drop	HEPES	50 (mM)	pH7.5
3	1	drop		50 (mM)
4	1	drop	dithiothreitol	1 (mM)
5	1	drop	EDTA	0.5 (mM)
6	1	drop	GTP	5 (mM)
7	1	reservoir	magnesium acetate	200 (mM)
8	1	reservoir	HEPES	100 (mM)	pH7.0
9	1	reservoir	PEG8000	18 (%(w/v))