1KI2

CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM HERPES SIMPLEX VIRUS TYPE I COMPLEXED WITH GANCICLOVIR

Experimental procedure

Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1995-04
Detector	RIGAKU RAXIS IIC
Spacegroup name	C 2 2 21
Unit cell lengths	114.900, 118.700, 109.100
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	12.000 - 2.200
R-factor	0.192
Rwork	0.192
R-free	0.29100
Structure solution method	MIR + NCS IMPROVEMENT AND SOLVENT FLATTENING FOR ORIGINAL NATIVE, 1KIN
RMSD bond length	0.012
RMSD bond angle	22.960 *
Data reduction software	R-AXIS ((HIGASHI/RIGAKU))
Data scaling software	PROCESS ((HIGASHI))
Phasing software	SOLOMON
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
High resolution limit [Å]	2.200	2.200 *
Rmerge	0.061 *
Number of reflections	28516
Completeness [%]	74.6	46 *
Redundancy	2.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5	25 *	drop consists of equal volume of protein and reservoir solutions *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	1.0 (mg/ml)
2	1	drop	Tris-Cl	40 (mM)
3	1	drop	dithiothreitol	3 (mM)
4	1	drop	deoxythymidine	0.2 (mM)
5	1	reservoir	ammonium sulfate	30 (%sat)
6	1	reservoir	Tris-Cl	200 (mM)
7	1	reservoir	dithiothreitol	3 (mM)
8	1	reservoir	deoxythymidine	0.2 (mM)