3E1H

Crystal structure of a type III polyketide synthase PKSIIINc from Neurospora crassa

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	6.8	295	PEG 8000, Isopropanol, Sodium acetate, HEPES, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 295K

Crystal Properties
Matthews coefficient	Solvent content
1.96	37.17

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 70.023	α = 90
b = 104.96	β = 90
c = 105.68	γ = 90

Symmetry
Space Group	P 21 21 21

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	MAR scanner 345 mm plate	Osmic mirrors	2007-07-27	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU RUH3R	1.5418

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (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	2.58	25	97.6	0.091		4.4	24396	24396

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
	2.58	2.67	88.2		0.387	2.24	3.5	2150

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	Resolution (High)	Resolution (Low)	Number Reflections (All)	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	PDB ENTRY 1CGZ and 1TED	2.58	25	23093	23093	1229	97.99	0.21593	0.21346	0.26016	RANDOM	32.068

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]
0.57			-1.45		0.88

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	39.499
r_dihedral_angle_3_deg	18.098
r_dihedral_angle_4_deg	16.782
r_dihedral_angle_1_deg	6.021
r_scangle_it	1.931
r_angle_refined_deg	1.361
r_scbond_it	1.172
r_mcangle_it	0.937
r_mcbond_it	0.522
r_nbtor_refined	0.304

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	39.499
r_dihedral_angle_3_deg	18.098
r_dihedral_angle_4_deg	16.782
r_dihedral_angle_1_deg	6.021
r_scangle_it	1.931
r_angle_refined_deg	1.361
r_scbond_it	1.172
r_mcangle_it	0.937
r_mcbond_it	0.522
r_nbtor_refined	0.304
r_nbd_refined	0.231
r_symmetry_hbond_refined	0.193
r_symmetry_vdw_refined	0.187
r_xyhbond_nbd_refined	0.162
r_chiral_restr	0.086
r_bond_refined_d	0.009
r_gen_planes_refined	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	5768
Nucleic Acid Atoms
Solvent Atoms	413
Heterogen Atoms

Software

Software
Software Name	Purpose
REFMAC	refinement
DENZO	data reduction
SCALEPACK	data scaling
MOLREP	phasing

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 R01GM133198.