4ALZ

The Yersinia T3SS basal body component YscD reveals a different structural periplasmatic domain organization to known homologue PrgH

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.1
Synchrotron site	BESSY
Beamline	14.1
Temperature [K]	100
Detector technology	CCD
Collection date	2011-06-16
Detector	MARMOSAIC 225 mm CCD
Spacegroup name	P 1 21 1
Unit cell lengths	37.990, 51.550, 50.630
Unit cell angles	90.00, 106.08, 90.00

Refinement procedure

Resolution	29.791 - 1.400
R-factor	0.1912
Rwork	0.189
R-free	0.22580
Structure solution method	OTHER
Starting model (for MR)	NONE
RMSD bond length	0.009
RMSD bond angle	1.238
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	Auto-Rickshaw
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.800	1.480
High resolution limit [Å]	1.400	1.400
Rmerge	0.040	0.550
Number of reflections	36930
<I/σ(I)>	21	2.3
Completeness [%]	95.5	99.7
Redundancy	3.7	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		292	YSCD150-347 G283P CRYSTALS GREW FROM EQUAL VOLUMES OF PROTEIN (5.8 MG/ML IN 20 MM HEPES PH 7.0, 60 MM NACL) WITH PRECIPITANT SOLUTION (0.15 M NAH2PO4, 20 % (W/V) PEG 3350, 60 MM NACL) IN HANGING-DROP VAPOR-DIFFUSION CRYSTALLIZATION TRAYS AT 292 K (EASYXTAL; QIAGEN).