6WDU

The external aldimine form of the Salmonella thypi wild-type tryptophan synthase in open conformation showing multiple side chain conformations for the residue beta Q114 and sodium ion at the metal coordination site. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 12.3.1
Synchrotron site	ALS
Beamline	12.3.1
Temperature [K]	100
Detector technology	CCD
Collection date	2019-04-18
Detector	ADSC QUANTUM 315r
Wavelength(s)	1.0000
Spacegroup name	C 1 2 1
Unit cell lengths	182.655, 59.415, 67.345
Unit cell angles	90.00, 94.89, 90.00

Refinement procedure

Resolution	36.910 - 1.400
R-factor	0.1634
Rwork	0.162
R-free	0.19490
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4hn4
RMSD bond length	0.008
RMSD bond angle	1.526
Data scaling software	SCALA (3.3.22)
Phasing software	PHASER (2.8.3)
Refinement software	REFMAC (5.8.0258)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	90.995	36.880	1.480
High resolution limit [Å]	1.398	4.430	1.400
Rmerge		0.042	0.920
Rmeas	0.102	0.046	1.014
Rpim	0.042	0.018	0.418
Total number of observations	793906	27405	107971
Number of reflections	141196	4528	20297
<I/σ(I)>	9	23.7	1.5
Completeness [%]	99.6	97.5	98.4
Redundancy	5.6	6.1	5.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.8	293	50 mM Bicine-NaOH, 10% PEG 8,000, 2 mM Spermine, pH 7.8, 50mM NaCl