1RSV

azide complex of the diferrous E238A mutant R2 subunit of ribonucleotide reductase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM1A
Synchrotron site	ESRF
Beamline	BM1A
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1992-09-22
Detector	MARRESEARCH
Wavelength(s)	1.00
Spacegroup name	P 21 21 21
Unit cell lengths	73.893, 84.501, 113.963
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	17.000 - 2.200
R-factor	0.18 *
Rwork	0.182
R-free	0.25600
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.019
RMSD bond angle	2.100
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	TNT
Refinement software	TNT

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	17.000	2.240
High resolution limit [Å]	2.200	2.200
Rmerge	0.123 *
Total number of observations	123580 *
Number of reflections	36078
Completeness [%]	97.3	97.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	20 *	Nordlund, P., (1989) FEBS Lett., 258, 251. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir	PEG4000	20 (%)
3	1	reservoir		0.2 (M)
4	1	reservoir	dioxane	0.3 (%)
5	1	reservoir	MES	0.05 (M)	pH6.0