4DLF

Crystal structure of an amidohydrolase (COG3618) from burkholderia multivorans (TARGET EFI-500235) with bound ZN, 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 315r
Wavelength(s)	0.9793
Spacegroup name	P 32 2 1
Unit cell lengths	75.300, 75.300, 142.450
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	38.386 - 1.925
R-factor	0.1944
Rwork	0.193
R-free	0.22820
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4dnm
RMSD bond length	0.012
RMSD bond angle	1.082
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]	65.212	38.386	2.030
High resolution limit [Å]	1.925	6.090	1.920
Rmerge		0.021	0.021
Total number of observations		7068	29620
Number of reflections	36087
<I/σ(I)>	7.3	10.5	0.4
Completeness [%]	99.8	98.3	99.9
Redundancy	5.9	5.7	5.7

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 D-arabonate-1,4-lactone; Reservoir (20% Peg3350, 100 mM HEPES pH 7.5); Cryoprotection (Reservoir, 5 mM Zn, 25 mM D-arabonate-1,4-lactone, 20% glycerol), sitting drop vapor diffuction, temperature 298K