1F3F

STRUCTURE OF THE H122G NUCLEOSIDE DIPHOSPHATE KINASE / D4T-TRIPHOSPHATE.MG COMPLEX

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LURE BEAMLINE D41A
Synchrotron site	LURE
Beamline	D41A
Temperature [K]	100
Detector technology	IMAGE PLATE
Detector	MARRESEARCH
Spacegroup name	P 31 2 1
Unit cell lengths	70.018, 70.018, 152.098
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.730 - 1.850
R-factor	0.203
Rwork	0.203
R-free	0.23400
RMSD bond length	0.013
RMSD bond angle	22.900 *
Data reduction software	MOSFLM
Data scaling software	CCP4 ((SCALA))
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.730	1.970
High resolution limit [Å]	1.850	1.850
Rmerge	0.056 *	0.328
Number of reflections	37405 *
Completeness [%]	99.3 *	98.7
Redundancy	5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.5		pH 7.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	PEG400	19 (%)
2	1	drop	Tris-HCl	50 (mM)
3	1	drop		20 (mM)
4	1	drop	protein	6 (mg/ml)
5	1	drop	d4T triphosphate	7.5 (mM)
6	1	reservoir	PEG400	38 (%)