5HXZ

Structure-function analysis of functionally diverse members of the cyclic amide hydrolase family of Toblerone fold enzymes

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Synchrotron site	Australian Synchrotron
Beamline	MX2
Temperature [K]	100
Detector technology	CCD
Collection date	2014-03-30
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.95370
Spacegroup name	P 21 21 21
Unit cell lengths	81.630, 83.732, 215.102
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.300 - 2.360
R-factor	0.22578
Rwork	0.224
R-free	0.25516
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5hxu
RMSD bond length	0.006
RMSD bond angle	1.136
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	REFMAC (5.8.0135)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	45.300	2.420
High resolution limit [Å]	2.360	2.360
Number of reflections	61689
<I/σ(I)>	8	2.6
Completeness [%]	99.9	98.6
Redundancy	7.4	7.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	Protein was at 15 mg/mL; reservoir was 2.5 M ammonium sulfate, 0.1 M bis-tris at pH 6.5; vapor diffusion sitting drops of 150 nL plus 150 nL; done at 20 C.