1H0O

Cobalt substitution of mouse R2 ribonucleotide reductase to model the reactive diferrous state

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2001-03-15
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	75.900, 106.570, 91.620
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.200
R-factor	0.235
Rwork	0.235
R-free	0.28200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1xsm
RMSD bond length	0.010
RMSD bond angle	19.550 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS (1.0)

Data quality characteristics

	Overall
Low resolution limit [Å]	30.000
High resolution limit [Å]	2.200
Number of reflections	22045

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.7		0.1 M NA-ACETATE BUFFER PH4.7, 1.2 M NACL, 7.5 MG/ML APO-R2 PROTEIN. CRYSTALS WERE MADE BY CO-CRYSTALLISATION (3.8 EQV. CO2+)., pH 4.70

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7.5 (mg/ml)
2	1	reservoir	sodium acetate	0.1 (M)	pH4.7
3	1	reservoir		1.2 (M)