5TP4

Crystal structure of a hydantoinase/carbamoylase family amidase from Burkholderia ambifaria

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2016-08-18
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	42.530, 136.960, 164.580
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	43.992 - 1.700
R-factor	0.1613
Rwork	0.161
R-free	0.19130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5i4m
RMSD bond length	0.009
RMSD bond angle	1.004
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.740
High resolution limit [Å]	1.700	7.600	1.700
Rmerge	0.074	0.021	0.543
Rmeas	0.082	0.023	0.593
Total number of observations	639016
Number of reflections	106677	1356	7742
<I/σ(I)>	17.87	46.81	3.68
Completeness [%]	99.8	98.5	99.9
CC(1/2)	0.999	1.000	0.885

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	290	Rigaku Reagents Morpheus screen G2: 10% PEG8000, 20% ethylene glycol, 0.1 M MES/Imidazole pH 6.5, 0.02M sodium formate, 0.02M ammonium acetate, 0.02M trisodium citrate, 0.02M sodium potassium L-tartrate, 0.02M sodium oxamate; BuamA.12245.a.B1.PS37939 at 12.3 mg/ml, tray 274677 g2, puck icb9-10