1F1B

CRYSTAL STRUCTURE OF E. COLI ASPARTATE TRANSCARBAMOYLASE P268A MUTANT IN THE R-STATE IN THE PRESENCE OF N-PHOSPHONACETYL-L-ASPARTATE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	295
Detector technology	AREA DETECTOR
Collection date	1998-06-09
Detector	UCSD MARK III
Spacegroup name	P 3 2 1
Unit cell lengths	122.150, 122.150, 156.230
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	8.000 - 2.300
R-factor	0.196 *
Rwork	0.196
R-free	0.23200
RMSD bond length	0.013
RMSD bond angle	25.300 *
Data reduction software	SDMS
Data scaling software	SDMS
Phasing software	X-PLOR
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.480
High resolution limit [Å]	2.300	2.300
Rmerge	0.068	0.387
Number of reflections	58790
<I/σ(I)>	7
Completeness [%]	97.8	94
Redundancy	4.4	2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICRODIALYSIS	5.75	20 *	ENZYME: 7.5 mg/ml in 50 uL microdialysis button. BUFFER: 20 mm maleic acid, 3 mM sodium azide, 1 mM N-phosphonacetyl-L-aspartate, pH 5.75, MICRODIALYSIS, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	enzyme	7.5 (mg/ml)
2	1	2	PALA	1 (mM)
3	1	2	maleic acid	20 (mM)
4	1	2	sodium azide	3 (mM)