3K2K

Crystal structure of putative carboxypeptidase (YP_103406.1) from BURKHOLDERIA MALLEI ATCC 23344 at 2.49 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL12-2
Synchrotron site	SSRL
Beamline	BL12-2
Temperature [K]	100
Detector technology	CCD
Collection date	2009-05-07
Detector	MARMOSAIC 325 mm CCD
Spacegroup name	I 41 2 2
Unit cell lengths	162.375, 162.375, 148.397
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.553 - 2.490
R-factor	0.157
Rwork	0.156
R-free	0.18500
Structure solution method	SAD
RMSD bond length	0.015
RMSD bond angle	1.563
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	SHELX
Refinement software	REFMAC (5.5.0053)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.553	29.553	2.580
High resolution limit [Å]	2.490	5.330	2.490
Rmerge	0.076	0.035	0.780
Number of reflections	34624	6757	6209
<I/σ(I)>	15.45	35.6	2.1
Completeness [%]	99.1	99.4	92

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	4.3000M NaCl, 0.1M HEPES pH 7.5, Additive: 0.006 M calcium chloride, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 293K