6CXD

Crystal structure of peptidase B from Yersinia pestis CO92 at 2.75 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2016-04-18
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	H 3 2
Unit cell lengths	101.558, 101.558, 240.475
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	50.000 - 2.750
R-factor	0.18097
Rwork	0.178
R-free	0.24925
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ij3
RMSD bond length	0.006
RMSD bond angle	1.032
Data reduction software	HKL-3000 (v716.4)
Data scaling software	HKL-3000 (v716.4)
Phasing software	HKL-3000 (v716.4)
Refinement software	REFMAC (5.8.0218)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.800
High resolution limit [Å]	2.750	2.750
Rmerge	0.152	0.666
Number of reflections	12769	600
<I/σ(I)>	16.5	1.8
Completeness [%]	99.5	94.8
Redundancy	10.8	5.9
CC(1/2)		0.928

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	289	0.2 uL 14 mg/mL protein in 20 mM Tris-HCl pH 7.5, 150 mM sodium chloride, 10% glycerol, 0.1% sodium azide, 0.5 mM TCEP, 1 mM ZnCl2 + 0.2 uL TOP96 #29 (0.2 M ammonium sulfate, 0.1 M sodium cacodylate, 30% w/v PEG8000) against 1.5 M sodium chloride, 96-well 3-drop crystallization plate (Swissci)