2FZM

Structure of the E. coli PutA proline dehydrogenase domain reduced by dithionite and complexed with SO2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	173
Detector technology	CCD
Collection date	2003-11-15
Detector	ADSC QUANTUM 4
Wavelength(s)	0.97856
Spacegroup name	I 2 2 2
Unit cell lengths	73.110, 141.424, 145.700
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.130 - 2.300
R-factor	0.212
Rwork	0.209
R-free	0.25700
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	: 1TJ0
RMSD bond length	0.015
RMSD bond angle	1.446
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.380
High resolution limit [Å]	2.300	4.950	2.300
Rmerge	0.071	0.035	0.465
Number of reflections	33078	3359	3129
<I/σ(I)>	9.7
Completeness [%]	98.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.7	293	Crystals were grown in 13-15% PEG 3350, 60-190 mM citrate buffer. Prior to data collection a crystal was soaked in excess Na dithionite in order to reduce the FAD cofactor., pH 5.7, VAPOR DIFFUSION, SITTING DROP, temperature 293K