2G85

Crystal structure of chorismate synthase from Mycobacterium tuberculosis at 2.22 angstrons of resolution

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7.8	293	0.1M Hepes-Na pH 7.8 buffer, 4M sodim chlorate , VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
4.62	73.39

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 130.288	α = 90
b = 130.288	β = 90
c = 157.95	γ = 120

Symmetry
Space Group	P 64 2 2

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	100	IMAGE PLATE	RIGAKU		2005-05-05	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	LNLS BEAMLINE D03B-MX1	1.427	LNLS	D03B-MX1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	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	2.22	50.25	99.4			37755	37564	2	1

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.22	2.34	22			4.5	5036

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	Resolution (High)	Resolution (Low)	Cut-off Sigma (F)	Number Reflections (All)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	PDB ENTRY 1ZTB	2.22	47.73	2	39553	35623	1873	94.8	0.17528	0.1732	0.17318	0.21441	RANDOM	33.825

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]
-0.01			-0.01		0.01

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	32.781
r_dihedral_angle_4_deg	26.51
r_dihedral_angle_3_deg	22.299
r_dihedral_angle_1_deg	8.73
r_scangle_it	6.025
r_scbond_it	3.972
r_mcangle_it	2.389
r_angle_refined_deg	2.286
r_mcbond_it	1.485
r_symmetry_hbond_refined	0.455

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	32.781
r_dihedral_angle_4_deg	26.51
r_dihedral_angle_3_deg	22.299
r_dihedral_angle_1_deg	8.73
r_scangle_it	6.025
r_scbond_it	3.972
r_mcangle_it	2.389
r_angle_refined_deg	2.286
r_mcbond_it	1.485
r_symmetry_hbond_refined	0.455
r_xyhbond_nbd_refined	0.33
r_nbtor_refined	0.326
r_symmetry_vdw_refined	0.307
r_nbd_refined	0.305
r_chiral_restr	0.204
r_bond_refined_d	0.017
r_gen_planes_refined	0.01

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2829
Nucleic Acid Atoms
Solvent Atoms	421
Heterogen Atoms

Software

Software
Software Name	Purpose
REFMAC	refinement
MOSFLM	data reduction
CCP4	data scaling
AMoRE	phasing

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.