1E19

Structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic archaeon Pyrococcus furiosus bound to ADP

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF
Synchrotron site	ESRF
Temperature [K]	100
Detector technology	CCD
Collection date	1998-09-15
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	55.400, 91.700, 133.800
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 1.500
R-factor	0.183 *
Rwork	0.183
R-free	0.21800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1b7b
RMSD bond length	0.020
RMSD bond angle	9.900 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	76.670	1.590
High resolution limit [Å]	1.430	1.500
Rmerge	0.067	0.355
Total number of observations	448640 *
Number of reflections	116569
<I/σ(I)>	5.2	1.9
Completeness [%]	97.3	98.6
Redundancy	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8.5 *	22 *	1.3M SODIUM CITRATE 0.1M TRIS-HCL, PH=8.5, 0-10% ETHYLENE GLYCOL PROTEIN SOLUTION: 10MG/ML OF PROTEIN IN 10MM TRIS-HCL CONTAINING 20MM ATP AND MGCL2, pH 8.00

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	Tris-HCl	50 (mM)
2	1	drop	ATP	20 (mM)
3	1	drop		20 (mM)
4	1	reservoir	sodium citrate	1.3 (M)
5	1	reservoir	Tris-HCl	0.1 (M)	pH8.5