1H7B

Structural basis for allosteric substrate specificity regulation in class III ribonucleotide reductases, native NRDD

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I711
Synchrotron site	MAX II
Beamline	I711
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-12-01
Detector	MAR scanner 345 mm plate
Spacegroup name	P 43 21 2
Unit cell lengths	98.019, 98.019, 242.421
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 * - 2.450
R-factor	0.229 *
Rwork	0.224
R-free	0.26000 *
Structure solution method	MIR
RMSD bond length	0.013 *
RMSD bond angle	23.400 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CCP4
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.460
High resolution limit [Å]	2.450 *	2.420
Rmerge	0.076	0.269
Number of reflections	43746
<I/σ(I)>	24.3	4
Completeness [%]	95.0	96.4
Redundancy	4.5 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5		Logan, D.T., (1999) Science, 283, 1499. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	HEPES-NaOH	0.1 (M)	pH7.5
2	1	reservoir		0.2 (M)
3	1	reservoir	dithiothreitol	5-7 (mM)
4	1	reservoir	PEG400	26-32 (%)
5	1	drop	protein	20-30 (mg/ml)