7MQV

Crystal structure of truncated (ACT domain removed) prephenate dehydrogenase tyrA from Bacillus anthracis in complex with NAD

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 19-BM
Synchrotron site	APS
Beamline	19-BM
Temperature [K]	100
Detector technology	CCD
Collection date	2020-03-04
Detector	ADSC QUANTUM 315r
Wavelength(s)	0.97929
Spacegroup name	P 1 21 1
Unit cell lengths	73.774, 118.882, 75.558
Unit cell angles	90.00, 92.39, 90.00

Refinement procedure

Resolution	49.120 - 2.400
R-factor	0.1692
Rwork	0.167
R-free	0.21550
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	6u60
RMSD bond length	0.008
RMSD bond angle	1.441
Data reduction software	HKL-3000
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0267)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.440
High resolution limit [Å]	2.400	6.510	2.400
Rmerge	0.114	0.028	0.866
Rmeas	0.137	0.034	1.053
Rpim	0.076	0.019	0.591
Number of reflections	51186	2636	2508
<I/σ(I)>	5.6
Completeness [%]	99.7	99.9	98.2
Redundancy	3.1	3.1	2.9
CC(1/2)		0.997	0.481

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	0.2 ul of 6 mg/ml protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 5% Glycerol, 10 mM BME, 5 mM NAD and 5 mM Tyrosine were mixed with 0.2 ul of the MCSG Suite 2 condition #46 (20%w/v PEG 3350, 0.2M Li citrate ) and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci).