1XJF

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

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	100
Detector technology	CCD
Collection date	2002-02-17
Detector	MARRESEARCH
Wavelength(s)	1.076
Spacegroup name	C 1 2 1
Unit cell lengths	116.300, 123.760, 107.030
Unit cell angles	90.00, 103.82, 90.00

Refinement procedure

Resolution	22.880 - 2.400
R-factor	0.21105
Rwork	0.208
R-free	0.26026
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rlr
RMSD bond length	0.016
RMSD bond angle	1.651
Data scaling software	CCP4 ((TRUNCATE))
Phasing software	CNS
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.600
High resolution limit [Å]	2.400	2.400
Number of reflections	57137
<I/σ(I)>	12.1	3.2
Completeness [%]	99.3	99.5
Redundancy	3.75

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