4DO7

Crystal structure of an amidohydrolase (cog3618) from burkholderia multivorans (target efi-500235) with bound zn, space group c2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 31-ID
Synchrotron site	APS
Beamline	31-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2011-11-15
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	C 1 2 1
Unit cell lengths	103.332, 76.728, 82.862
Unit cell angles	90.00, 117.67, 90.00

Refinement procedure

Resolution	30.626 - 1.700
R-factor	0.1777
Rwork	0.176
R-free	0.20910
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4dnm
RMSD bond length	0.007
RMSD bond angle	1.021
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.16)
Phasing software	PHENIX
Refinement software	PHENIX (1.7.3_928)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	73.388	40.383	1.790
High resolution limit [Å]	1.700	5.380	1.700
Rmerge		0.036	0.399
Total number of observations		6988	29480
Number of reflections	62061
<I/σ(I)>	10.7	15.3	2
Completeness [%]	98.5	94.3	98.9
Redundancy	3.5	3.6	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	sitting drop vapor diffuction	7.5	298	Protein (10 mM Hepes, pH 7.8, 150 mM NaCl, 10% glycerol, 0.5 mM ZnCl, 0.5 mM Fuconate 1,4-lactone; Reservoir (1.26 M AmmSO4, 100 mM HEPES pH 7.5); Cryoprotection (Reservoir, + 20% glycerol), sitting drop vapor diffuction, temperature 298K