5V1T

Crystal structure of Streptococcus suis SuiB bound to precursor peptide SuiA

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-B
Synchrotron site	APS
Beamline	23-ID-B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2015-07-20
Detector	MAR scanner 300 mm plate
Wavelength(s)	1.0332
Spacegroup name	P 21 21 2
Unit cell lengths	69.370, 115.040, 54.330
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.235 - 2.100
R-factor	0.1926
Rwork	0.189
R-free	0.22270
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5v1q
RMSD bond length	0.006
RMSD bond angle	0.942
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHENIX
Refinement software	PHENIX ((1.10.1_2155: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.240	2.160
High resolution limit [Å]	2.100	2.100
Rmerge	0.123	0.799
Number of reflections	25903
<I/σ(I)>	9.3	1.9
Completeness [%]	99.3	97.1
Redundancy	3.4	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		285	A solution containing 23 mg/mL of His6-tagged SuiB in storage buffer [100 mM HEPES, pH 7.5, 300 mM KCl, 5 mM DTT, 10% (v/v) glycerol] was mixed with a stock solution of SuiA in storage buffer lacking DTT, yielding a final SuiA concentration of 1.9 mM. The resultant solution was incubated for 10 min after which it was combined 1:1 with precipitant solution to form a 4 uL drop. Crystals appeared within 2 days and were fully grown within a week. The precipitant solution was generated by combining 100 mM Bis-Tris, pH 6.0, 200 mM Li2SO4, 27% (w/v) PEG 3350 with 210 mM SAM in water to yield a final SAM concentration of 10.5 mM.