2TOD

ORNITHINE DECARBOXYLASE FROM TRYPANOSOMA BRUCEI K69A MUTANT IN COMPLEX WITH ALPHA-DIFLUOROMETHYLORNITHINE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE A1
Synchrotron site	CHESS
Beamline	A1
Temperature [K]	90
Spacegroup name	P 1 21 1
Unit cell lengths	66.800, 154.500, 77.100
Unit cell angles	90.00, 90.58, 90.00

Refinement procedure

Resolution	8.000 - 2.000
R-factor	0.212 *
Rwork	0.212
R-free	0.27000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7odc
RMSD bond length	0.016 *
RMSD bond angle	0.041 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000
High resolution limit [Å]	2.000
Rmerge	0.090
Total number of observations	339850 *
Number of reflections	103282
<I/σ(I)>	13.9
Completeness [%]	97.6	61.7 *
Redundancy	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8 *	16 *	Grishin, N.V., (1996) Proteins Struct. Funct. Genet., 24, 272. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	PEG3350	20 (%)
2	1	drop	Tris-HCl	0.1 (M)
3	1	drop	ammonium acetate	0.2 (M)
4	1	drop	dithiothreitol	10 (mM)
5	1	drop	protain	20 (mg/ml)