1R1R

RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI

Experimental procedure

Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	278
Detector technology	IMAGE PLATE
Collection date	1995-06
Detector	MARRESEARCH
Spacegroup name	H 3 2
Unit cell lengths	227.820, 227.820, 343.470
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 2.900
R-factor	0.22
Rwork	0.210
R-free	0.24500
Structure solution method	RIGID BODY
RMSD bond length	0.007 *
RMSD bond angle	1.700 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	TNT
Refinement software	TNT

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.000
High resolution limit [Å]	2.900	2.900
Rmerge	0.087	0.373 *
Number of reflections	77589
<I/σ(I)>	15.6	2.7
Completeness [%]	96.0	52.2 *
Redundancy	3.3	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6		Uhlin, U., (1993) FEBS Lett., 336, 148. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	lithium sulphate	17 (%)
2	1	reservoir	magnesium sulphate	10 (mM)
3	1	reservoir	sodium citrate	25 (mM)	pH6.0
4	1	drop	protein	30 (mg/ml)
5	1	drop	peptide solution	15 (mg/ml)