7ODC

CRYSTAL STRUCTURE ORNITHINE DECARBOXYLASE FROM MOUSE, TRUNCATED 37 RESIDUES FROM THE C-TERMINUS, TO 1.6 ANGSTROM RESOLUTION

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE F1
Synchrotron site	CHESS
Beamline	F1
Temperature [K]	98
Detector technology	CCD
Collection date	1996-09
Spacegroup name	P 21 21 2
Unit cell lengths	118.500, 74.000, 45.600
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	27.900 - 1.600
R-factor	0.2 *
Rwork	0.199
R-free	0.23200
Structure solution method	MIR
RMSD bond length	0.010 *
RMSD bond angle	2.188 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MLPHARE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	27.920	1.660
High resolution limit [Å]	1.600	1.600
Rmerge	0.081	0.188
Number of reflections	49125
<I/σ(I)>		3.5
Completeness [%]	91.3	75.4
Redundancy	5	1.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	6.5		combination of vapor diffusion and gel *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	12 (mg/ml)
2	1	drop	dithiothreitol	2.5 (mM)
3	1	drop	EDTA	1.0 (mM)
4	1	drop	PEG3350	26 (%(w/v))
5	1	reservoir	PEG3350	10 (%(w/v))