5UYY

Crystal structure of prephenate dehydrogenase tyrA from Bacillus anthracis in complex with L-tyrosine

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	2014-07-24
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	P 21 21 21
Unit cell lengths	84.682, 105.588, 179.625
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.600
R-factor	0.1913
Rwork	0.189
R-free	0.24610
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ggg
RMSD bond length	0.016
RMSD bond angle	1.732
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0107)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.640
High resolution limit [Å]	2.600	7.050	2.600
Rmerge	0.069	0.028	0.963
Rmeas	0.071	0.031
Rpim	0.027	0.012	0.374
Number of reflections	50884		2499
<I/σ(I)>	8.2		2.1
Completeness [%]	99.9	99.1	100
Redundancy	7.4	6.5	7.5
CC(1/2)		0.999	0.803

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	289	0.2 ul of 19 mg/ml protein in 20 mM HEPES pH 7.5, 150 mM NaCl, 5% Glycerol, and 10 mM BME were mixed with 0.2 ul of the MCSG Suite 1 condition #11 (0.1 M MES pH=6.5, 0.2 M Magnesium chloride, 10% w/v PEG 4000) and equilibrated against 1.5 M NaCl solution in 96 Well 3 drop Crystallization Plate (Swissci). His-tag was removed prior to crystallization.