1XSM

PROTEIN R2 OF RIBONUCLEOTIDE REDUCTASE FROM MOUSE

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.6
Synchrotron site	SRS
Beamline	PX9.6
Temperature [K]	277
Detector technology	IMAGE PLATE
Collection date	1992-02-15
Detector	RIGAKU RAXIS IIC
Spacegroup name	C 2 2 21
Unit cell lengths	77.078, 108.932, 92.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.000 - 2.300
R-factor	0.191
Rwork	0.191
R-free	0.25000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1rib
RMSD bond length	0.018
RMSD bond angle	28.600 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	2.380
High resolution limit [Å]	2.300	2.290
Rmerge	0.104	0.300 *
Total number of observations	144719 *
Number of reflections	17131
<I/σ(I)>	17.6
Completeness [%]	95.8 *	70.9
Redundancy	8.8	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.7	20 *	Nielsen, B.B., (1995) FEBS Letters, 373, 310. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7.5 (mg/ml)
2	1	drop		0.8-1.0 (M)
3	1	drop	acetate	50 (mM)
4	1	reservoir		0.8-1.0 (M)
5	1	reservoir	acetate	50 (mM)