1XJG

Structural mechanism of allosteric substrate specificity in a ribonucleotide reductase: dATP-UDP complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X13
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X13
Temperature [K]	100
Detector technology	CCD
Collection date	2003-06-28
Detector	MARRESEARCH
Wavelength(s)	0.803
Spacegroup name	C 1 2 1
Unit cell lengths	118.537, 123.514, 105.886
Unit cell angles	90.00, 102.60, 90.00

Refinement procedure

Resolution	24.870 - 2.500
R-factor	0.19816
Rwork	0.195
R-free	0.26366
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1xje
RMSD bond length	0.019
RMSD bond angle	1.940
Data scaling software	SCALEPACK
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.560
High resolution limit [Å]	2.500	2.500
Number of reflections	48781
<I/σ(I)>	21.5	3.77
Completeness [%]	99.9	100
Redundancy	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	4.5	293	PEG8000, sodium acetate, sodium chloride, dithiotreithol, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K