1E2K

Kinetics and crystal structure of the wild-type and the engineered Y101F mutant of Herpes simplex virus type 1 thymidine kinase interacting with (North)-methanocarba-thymidine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE BW7B
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	BW7B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-03-12
Detector	MARRESEARCH
Spacegroup name	C 2 2 21
Unit cell lengths	114.000, 117.700, 108.200
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.700
R-factor	0.209 *
Rwork	0.209
R-free	0.25200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1vtk
RMSD bond length	0.017
RMSD bond angle	0.025
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.800
High resolution limit [Å]	1.700	1.700
Rmerge	0.050	0.580
Number of reflections	79549
<I/σ(I)>	15	2.1
Completeness [%]	99.0	99
Redundancy	4.1	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	8 *	23 *	LITHIUM SULFATE, HEPES, DTT, pH 7.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	25 (mg/ml)
2	1	reservoir		0.9-1.2 (M)
3	1	reservoir	dithiothreitol	1 (mM)
4	1	reservoir	HEPES	0.1 (M)