6CTY

Crystal structure of dihydroorotase pyrC from Yersinia pestis in complex with zinc and malate at 2.4 A resolution

Replaces:  5V0G

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-ID
Synchrotron site	APS
Beamline	19-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2016-11-12
Detector	DECTRIS PILATUS3 X 6M
Wavelength(s)	0.97923, 1.28241, 1.28908
Spacegroup name	P 21 21 21
Unit cell lengths	95.838, 112.202, 208.264
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.010 - 2.410
R-factor	0.1613
Rwork	0.159
R-free	0.19790
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2eg6
RMSD bond length	0.009
RMSD bond angle	1.209
Data reduction software	HKL-3000
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0158)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.010	50.000	2.440
High resolution limit [Å]	2.400	6.510	2.400
Rmerge	0.088	0.036	0.622
Rmeas	0.096	0.039	0.680
Rpim	0.037	0.015	0.265
Number of reflections	81980	4625	4079
<I/σ(I)>	7.5		2.1
Completeness [%]	93.8	98.6	94.1
Redundancy	6.1	5.9	6
CC(1/2)		0.997	0.778

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	289	0.2 uL 10 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 + 0.2 uL MCSG 2 condition #67 (0.15 M DL-malic acid, pH 7.0, 20% w/v PEG3350), equilibrated against 1.3 M sodium chloride solution in 96-well 3-drop crystallization plate (Swissci)