2FZN

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

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	73.115, 143.221, 145.124
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	22.700 - 2.000
R-factor	0.216
Rwork	0.214
R-free	0.25100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	: 1TJ0
RMSD bond length	0.014
RMSD bond angle	1.413
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	27.000	27.000	2.070
High resolution limit [Å]	2.000	4.300	2.000
Rmerge	0.061	0.029	0.419
Number of reflections	51335	5075	4706
<I/σ(I)>	12.3
Completeness [%]	98.1
Redundancy	5.7	5.5	4.7

Crystallization Conditions

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