4CQC

The reaction mechanism of the N-isopropylammelide isopropylaminohydrolase AtzC: insights from structural and mutagenesis studies

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	2013-12-14
Detector	ADSC CCD
Spacegroup name	C 1 2 1
Unit cell lengths	106.234, 87.280, 114.364
Unit cell angles	90.00, 103.93, 90.00

Refinement procedure

Resolution	46.370 - 2.200
R-factor	0.19695
Rwork	0.196
R-free	0.22311
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2qt3
RMSD bond length	0.010
RMSD bond angle	1.269
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	REFMAC (5.7.0032)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	46.300	2.320
High resolution limit [Å]	2.200	2.200
Rmerge	0.140	0.800
Number of reflections	51202
<I/σ(I)>	12.5	2.8
Completeness [%]	99.4	98.9
Redundancy	7.7	7.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1		7.5		PROTEIN AT 5.5 MG/ML OVER A RESERVOIR OF 2.5 M MALONATE PH 7.0, 100 MM HEPES BUFFER AT PH 7.5; DROPS WERE 150 NL PLUS 150 NL. IN-SITU THROMBIN TREATMENT WAS USED TO REMOVE THE HIS-TAG.