1FMK

CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC

Experimental procedure

Spacegroup name	P 21 21 21
Unit cell lengths	51.759, 87.380, 101.295
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 1.500
R-factor	0.21
Rwork	0.210
R-free	0.26400
Structure solution method	MULTIPLE ISOMORPHOUS HEAVY-ATOM REPLACEMENT (MIR) METHOD. THREE DERIVATIVES USED FOR PHASING.
RMSD bond length	0.010
RMSD bond angle	1.160
Phasing software	X-PLOR
Refinement software	X-PLOR

Data quality characteristics

	Overall
Low resolution limit [Å]	20.000
High resolution limit [Å]	1.500
Rmerge	0.053 *
Total number of observations	102852 *
Number of reflections	25752 *
Completeness [%]	90.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.5 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	15 (mg/ml)
2	1	reservoir	PIPES	50 (mM)
3	1	reservoir	sodium tartrate	0.8 (M)
4	1	reservoir	dithiothreitol	20 (mM)