5THW

Crystal structure of Amidase, hydantoinase/carbamoylase family from Burkholderia multivorans

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	2016-06-08
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	86.460, 88.510, 126.440
Unit cell angles	90.00, 90.21, 90.00

Refinement procedure

Resolution	39.394 - 2.500
R-factor	0.1564
Rwork	0.155
R-free	0.21220
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5i4m
RMSD bond length	0.005
RMSD bond angle	0.735
Data reduction software	XDS
Data scaling software	XDS
Phasing software	MOLREP
Refinement software	PHENIX ((1.11rc1_2513: ???))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.560
High resolution limit [Å]	2.500	11.180	2.500
Rmerge	0.080	0.024	0.494
Number of reflections	65364
<I/σ(I)>	14.21	38.79	2.89
Completeness [%]	98.6	94.3	98.2
Redundancy	3.86
CC(1/2)	0.997	0.999	0.820

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	RigakuReagents JCSG+ screen, B2: 25% PEG 3350, 200mM Sodium thiocyanate; BumuA.12245.e.B1.PW37879 at 19.5mg/ml; cryo: 20% EG; tray 272537b2, puck ujd4-3