1PFR

RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 BETA CHAIN

Experimental procedure

Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX9.5
Synchrotron site	SRS
Beamline	PX9.5
Temperature [K]	300
Detector technology	IMAGE PLATE
Collection date	1992-06
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	74.300, 85.500, 115.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.200
R-factor	0.179 *
Rwork	0.179
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	DIFERRIC FORM OF R2 PROTEIN PDB ENTRY 1RIB
RMSD bond length	0.011
RMSD bond angle	17.252 *
Data reduction software	MOSFLM
Data scaling software	CCP4
Phasing software	AMoRE
Refinement software	TNT (5E)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.260
High resolution limit [Å]	2.200	2.200
Rmerge	0.095	0.376
Total number of observations	95516 *
Number of reflections	34220 *
<I/σ(I)>	7.1	1.8
Completeness [%]	86.0	34.1
Redundancy	2.79	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6		HANGING DROP VAPOR DIFFUSION. CRYSTALLISED FROM 20% PEG 4000, 0.2M NACL, 0.1M MES PH 6.0, 1MM ETHYLMERCURY SALICYLATE., vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG4000	22 (%)
2	1	reservoir		0.2 (M)
3	1	reservoir	MES	50 (mM)
4	1	reservoir	ethylmercury thiosalicylate	1 (mM)