7R1R

RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS
Synchrotron site	NSLS
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1995-11
Detector	RIGAKU RAXIS IIC
Spacegroup name	H 3 2
Unit cell lengths	224.560, 224.560, 335.450
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 3.100
R-factor	0.205
Rwork	0.200
R-free	0.23100
Structure solution method	RIGID BODY
Starting model (for MR)	5r1r
RMSD bond length	0.010 *
RMSD bond angle	2.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	TNT
Refinement software	TNT

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	3.200
High resolution limit [Å]	3.100	3.100
Rmerge	0.078	0.360
Number of reflections	53836
<I/σ(I)>	14.1	1.9
Completeness [%]	91.3	81.4
Redundancy	2.7	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6		PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	17 (mg/ml)
2	1	reservoir	lithium sulfate	17 (%)
3	1	reservoir	magnesium sulfate	10 (mM)
4	1	reservoir	citrate	25 (mM)