2AY0

Structure of the Lys9Met mutant of the E. coli Proline Utilization A (PutA) DNA-binding domain.

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 4.2.2
Synchrotron site	ALS
Beamline	4.2.2
Temperature [K]	173
Detector technology	CCD
Collection date	2004-12-08
Detector	CUSTOM-MADE
Wavelength(s)	0.987121, 0.979553, 0.979144
Spacegroup name	C 1 2 1
Unit cell lengths	72.070, 91.494, 69.606
Unit cell angles	90.00, 119.21, 90.00

Refinement procedure

Resolution	60.750 - 2.100
R-factor	0.20597
Rwork	0.204
R-free	0.24180
Structure solution method	MAD
RMSD bond length	0.011
RMSD bond angle	1.139
Data scaling software	d*TREK (9.2LDz)
Phasing software	SOLVE (2.06)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	60.750	36.530	2.070
High resolution limit [Å]	2.000	4.310	2.000
Rmerge	0.079	0.060	0.520
Number of reflections	26606
<I/σ(I)>	12.5	26.4	3.7
Completeness [%]	100.0
Redundancy	7.47

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		295	1.7-3.0 M NaCl, 5 mM dithiothreitol, pH 3.0-5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
1	VAPOR DIFFUSION, HANGING DROP		295	1.7-3.0 M NaCl, 5 mM dithiothreitol, pH 3.0-5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
1	VAPOR DIFFUSION, HANGING DROP		295	1.7-3.0 M NaCl, 5 mM dithiothreitol, pH 3.0-5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K