1R6F

The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X9A
Synchrotron site	NSLS
Beamline	X9A
Temperature [K]	100
Detector technology	CCD
Collection date	2002-01-15
Detector	ADSC QUANTUM 4
Wavelength(s)	0.9795, 0.9790, 0.9719
Spacegroup name	P 1
Unit cell lengths	35.881, 45.086, 46.915
Unit cell angles	76.20, 78.42, 77.17

Refinement procedure

Resolution	30.000 * - 2.170
R-factor	0.224
Rwork	0.217
R-free	0.28400
Structure solution method	MAD
RMSD bond length	0.008
RMSD bond angle	1.877
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	SHARP
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	18.500	2.250
High resolution limit [Å]	2.170	2.170
Rmerge	0.077	0.370
Total number of observations	31607 *
Number of reflections	14116
<I/σ(I)>	12.5	2
Completeness [%]	95.9	86.2
Redundancy	2.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	8.7	294	PEG 5000 MME, sodium acetate, Tris, pH 8.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K
1	Vapor diffusion, sitting drop *	8.7	294	PEG 5000 MME, sodium acetate, Tris, pH 8.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG5000 MME	26 (%(w/v))
2	1	reservoir	sodium acetate	200 (mM)
3	1	reservoir	Tris-HCl	100 (mM)	pH8.7
4	1	drop	protein	30 (mg/ml)