5IZT

Crystal structure of a C-terminal proteolytic fragment of an outer surface protein from Borrelia burgdorferi

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	2016-03-11
Detector	RAYONIX MX-225
Wavelength(s)	0.97872
Spacegroup name	P 1
Unit cell lengths	31.340, 54.030, 66.960
Unit cell angles	101.44, 98.73, 85.00

Refinement procedure

Resolution	27.405 - 1.900
R-factor	0.1688
Rwork	0.166
R-free	0.21130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2yn7
RMSD bond length	0.006
RMSD bond angle	0.770
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((dev_2356))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.950
High resolution limit [Å]	1.900	8.500	1.900
Rmerge	0.054	0.026	0.482
Number of reflections	32761
<I/σ(I)>	17.18	41.93	3.06
Completeness [%]	97.7	95.7	96.3
Redundancy	3.92
CC(1/2)	0.998

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.6	290	Microlytic MCSG 1 screen H3: 20% PEG 4000, 20% iso-Propanol, 100mM Na3-citrate pH 5.6; BobuA.18967.a.B2.PW37767 at 20mg/ml; cryo: 20% EG; tray 266029 h3; puck rgo9-7