5CGQ

Crystal structure of Tryptophan Synthase from Salmonella typhimurium in complex with F9 ligand in the alpha-site and the product L-Tryptophan in the beta-site.

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	4HT3

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	7.6	298	50 mM Bicine-CsOH, pH 7.6, 10% PEG 8,000, 100 mM CsCl2, 1 mM spermine

Crystal Properties
Matthews coefficient	Solvent content
2.54	51.55

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 182.553	�� = 90
b = 59.3	�� = 94.82
c = 67.368	�� = 90

Symmetry
Space Group	C 1 2 1

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	100	CCD	ADSC QUANTUM 315		2012-05-04	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ALS BEAMLINE 12.3.1	1.0000	ALS	12.3.1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	R Sym I (Observed)	Rrim I (All)	Rpim I (All)	CC (Half)	Net I Over Average Sigma (I)	Redundancy	Number Reflections (All)	Number Reflections (Observed)	Observed Criterion Sigma (F)	Observed Criterion Sigma (I)	B (Isotropic) From Wilson Plot
1	1.18	40	98.6	0.081	0.081	0.086	0.028	0.999	14.7	9.3	231646	231646

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	R-Sym I (Observed)	Rpim I (All)	CC (Half)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.18	1.24	94.2		0.872	0.037	0.015	0.778	3	7.9	32187

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	Resolution (High)	Resolution (Low)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	4HT3	1.18	39.21	219965	11610	98.52	0.1414	0.1404	0.1605	RANDOM	17.768

Temperature Factor Modeling
Anisotropic B[1][1]	Anisotropic B[1][2]	Anisotropic B[1][3]	Anisotropic B[2][2]	Anisotropic B[2][3]	Anisotropic B[3][3]
0.08		0.44	-0.29		0.13

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.27
r_sphericity_free	18.535
r_dihedral_angle_4_deg	16.187
r_dihedral_angle_3_deg	11.607
r_sphericity_bonded	10.796
r_rigid_bond_restr	10.73
r_dihedral_angle_1_deg	5.81
r_scbond_it	1.784
r_mcangle_it	1.437
r_angle_refined_deg	1.406

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.27
r_sphericity_free	18.535
r_dihedral_angle_4_deg	16.187
r_dihedral_angle_3_deg	11.607
r_sphericity_bonded	10.796
r_rigid_bond_restr	10.73
r_dihedral_angle_1_deg	5.81
r_scbond_it	1.784
r_mcangle_it	1.437
r_angle_refined_deg	1.406
r_mcbond_it	1.186
r_chiral_restr	0.092
r_bond_refined_d	0.012
r_gen_planes_refined	0.008

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	4971
Nucleic Acid Atoms
Solvent Atoms	825
Heterogen Atoms	70

Software

Software
Software Name	Purpose
REFMAC	refinement
MOSFLM	data reduction
SCALA	data scaling
MOLREP	phasing
DM	phasing
PDB_EXTRACT	data extraction

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.