3HAZ

Crystal structure of bifunctional proline utilization A (PutA) protein

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 4.2.2
Synchrotron site	ALS
Beamline	4.2.2
Temperature [K]	100
Detector technology	CCD
Collection date	2007-05-02
Detector	NOIR-1
Wavelength(s)	1.000
Spacegroup name	C 1 2 1
Unit cell lengths	166.763, 195.846, 108.680
Unit cell angles	90.00, 121.48, 90.00

Refinement procedure

Resolution	42.330 - 2.100
R-factor	0.202
Rwork	0.200
R-free	0.23300
Structure solution method	combination of Se-Met MAD/SAD and MR
Starting model (for MR)	Partial model from MAD/SAD phasing from another crystal form
RMSD bond length	0.005
RMSD bond angle	0.860
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SOLVE
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	43.270	43.270	2.210
High resolution limit [Å]	2.100	6.640	2.100
Rmerge	0.103	0.070	0.412
Total number of observations		20641	93890
Number of reflections	172549
<I/σ(I)>	5.386	7.2	1.8
Completeness [%]	100.0	99.6	100
Redundancy	3.8	3.7	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	298	2M Ammonium sulfate, 0.1 M Tris-HCl pH 7.0. N-terminal His tag cleaved by TEV protease, which leaves Gly-His at N-terminus., VAPOR DIFFUSION, SITTING DROP, temperature 298K