4DNM

Crystal structure of an amidohydrolase (cog3618) from burkholderia multivorans (target efi-500235) with bound hepes, space group p3221

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X29A
Synchrotron site	NSLS
Beamline	X29A
Temperature [K]	100
Detector technology	CCD
Collection date	2011-10-15
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9793
Spacegroup name	P 32 2 1
Unit cell lengths	75.070, 75.070, 142.260
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	47.988 - 2.150
R-factor	0.1921
Rwork	0.190
R-free	0.22790
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.010
RMSD bond angle	1.110
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHENIX
Refinement software	PHENIX (1.7.3_928)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]		2.030
High resolution limit [Å]	1.930	1.930
Rmerge	0.124	1.984
Number of reflections	35866
<I/σ(I)>	13	1.4
Completeness [%]	99.9	99.9
Redundancy	11.4	11.3

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 (20% Peg3350, 100 mM HEPES pH 7.5, 9 mM TCEP); Cryoprotection (Reservoir, + 20% glycerol), sitting drop vapor diffuction, temperature 298K