5W15

Crystal structure of an alpha/beta hydrolase fold protein 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	2016-06-22
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	60.070, 143.590, 75.850
Unit cell angles	90.00, 111.34, 90.00

Refinement procedure

Resolution	50.000 - 1.750
R-factor	0.1662
Rwork	0.166
R-free	0.18780
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4k2a
RMSD bond length	0.006
RMSD bond angle	0.876
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHENIX
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.800
High resolution limit [Å]	1.750	7.830	1.750
Rmerge	0.068	0.031	0.565
Rmeas	0.076	0.035	0.633
Number of reflections	120204	1378	8866
<I/σ(I)>	14.92	35.82	2.73
Completeness [%]	99.8	98.5	99.9
Redundancy	5.082	4.902	4.933
CC(1/2)	0.998	0.998	0.835

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	290	JCGS+ B8 (283558b8): 100 mM Tris-HCl pH 7.0, 200 mM MgCl2, 10% PEG 8000, protein conc. 19. 9mg/mL, cryo 20% ethylene glycol: puck ID vkw3-6