4ZP1

Crystal structure of Zymomonas mobilis pyruvate decarboxylase variant Glu473Ala

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Synchrotron site	PETRA III, EMBL c/o DESY
Beamline	P13 (MX1)
Temperature [K]	100
Detector technology	PIXEL
Collection date	2014-04-03
Detector	PSI PILATUS 6M
Wavelength(s)	0.98420
Spacegroup name	P 1 21 1
Unit cell lengths	70.290, 167.640, 110.820
Unit cell angles	90.00, 101.66, 90.00

Refinement procedure

Resolution	47.545 - 2.205
R-factor	0.1721
Rwork	0.170
R-free	0.21660
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.005
RMSD bond angle	0.844
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	47.550		2.310
High resolution limit [Å]	2.200	50.000	2.200
Rmerge	0.061		0.559
Rmeas	0.071		0.656
Total number of observations	471480
Number of reflections	124039		15208
<I/σ(I)>	16.15		2.38
Completeness [%]	98.3		97.1
Redundancy	3.8		3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	277	ZmPDC variant Glu473Ala was concentrated to 7.5 mg/mL in 10 mM citrate buffer (pH 6.0) containing 1 mM ThDP and 1 mM MgSO4. 1 microL of the enzyme was mixed with 1 microL of the reservoir solution containing 100 mM Tris, 40 mM NiCl2, 15% PEG2000, 1 mM ThDP, 1 mM MgSO4, and 100 mM sodium malonate.