1S5O

Structural and Mutational Characterization of L-carnitine Binding to Human carnitine Acetyltransferase

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F1
Synchrotron site	CHESS
Beamline	F1
Temperature [K]	100
Detector technology	CCD
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9504
Spacegroup name	P 21 21 21
Unit cell lengths	137.560, 84.650, 57.370
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.800
R-factor	0.189
Rwork	0.189
R-free	0.22300 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1nm8
RMSD bond length	0.010
RMSD bond angle	1.300
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.860
High resolution limit [Å]	1.800	1.800
Rmerge	0.086 *	0.343 *
Number of reflections	58948
<I/σ(I)>	4.12
Completeness [%]	91.6	83.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	6.2	295	Bis-Tris, NaCl, PEG8000, L-Carnitine, hpCAT, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	L-carnitine	1 (mM)
3	1	reservoir	Bis-Tris	50 (mM)	pH6.2
4	1	reservoir		100 (mM)
5	1	reservoir	PEG8000	12-15 (%)