1H0N

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 ID14-3
Synchrotron site	ESRF
Beamline	ID14-3
Temperature [K]	100
Detector technology	CCD
Collection date	2001-04-15
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	75.100, 106.860, 91.460
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.400
R-factor	0.218
Rwork	0.218
R-free	0.29700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1xsm
RMSD bond length	0.024
RMSD bond angle	21.800 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.480
High resolution limit [Å]	2.400 *	2.370
Rmerge	0.095 *	0.410
Number of reflections	15274 *
<I/σ(I)>	9.6	3.71
Completeness [%]	99.3 *	99
Redundancy	2.4

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 SOAKED IN 5 MM CO2+ SOLUTION, PH INCREASED TO 6

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)