4EG0

Crystal Structure of D-alanine--D-alanine ligase from Burkholderia ambifaria

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.1
Synchrotron site	ALS
Beamline	5.0.1
Temperature [K]	100
Detector technology	CCD
Collection date	2012-03-03
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97740
Spacegroup name	P 1 21 1
Unit cell lengths	48.380, 118.110, 56.930
Unit cell angles	90.00, 91.56, 90.00

Refinement procedure

Resolution	40.978 - 1.650
R-factor	0.1747
Rwork	0.173
R-free	0.20010
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1iov
RMSD bond length	0.018
RMSD bond angle	1.740
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.7.3_928)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		1.690
High resolution limit [Å]	1.650	7.380	1.650
Rmerge	0.035	0.018	0.478
Number of reflections	76670	705	5542
<I/σ(I)>	17.57	50.71	2.29
Completeness [%]	94.9	79.6	97.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	290	Morpheus condition A12: 0.06 M magnesium chloride, 0.06 M calcium chloride, 0.1 M TRIS-Bicine, 37.5% MPD/PEG1000/PEG3350, 20.26 mg/ml BuamA.00119.a.A1 PS01236, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 290K