3TFO

Crystal structure of a putative 3-oxoacyl-(acyl-carrier-protein) reductase from Sinorhizobium meliloti

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	5.6	293	0.5 M Ammonium sulfate, 0.1M Sodium citrate tribasic dihydrate pH 5.6, 1M Lithium Sulfate monohydrate, 6% 1-6 hexanediol, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
3.13	60.7

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 108.551	α = 90
b = 108.551	β = 90
c = 207.314	γ = 120

Symmetry
Space Group	P 31 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	Mirrors	2011-08-12	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	NSLS BEAMLINE X29A	0.9792	NSLS	X29A

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	2.08	50	99.9	0.08	9	10.1	85345	85345

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)
1	2.08	2.15	100		0.386	5	10.5	8401

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	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	SAD	THROUGHOUT	2.08	48.08	85345	80985	4270	99.82	0.17823	0.17613	0.21858	RANDOM	32.572

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]
0.06	0.03		0.06		-0.08

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.723
r_dihedral_angle_4_deg	22.682
r_dihedral_angle_3_deg	16.486
r_scangle_it	7.087
r_dihedral_angle_1_deg	6.334
r_scbond_it	4.399
r_mcangle_it	2.418
r_angle_refined_deg	2.413
r_mcbond_it	1.413
r_chiral_restr	0.306

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.723
r_dihedral_angle_4_deg	22.682
r_dihedral_angle_3_deg	16.486
r_scangle_it	7.087
r_dihedral_angle_1_deg	6.334
r_scbond_it	4.399
r_mcangle_it	2.418
r_angle_refined_deg	2.413
r_mcbond_it	1.413
r_chiral_restr	0.306
r_bond_refined_d	0.032
r_gen_planes_refined	0.011

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	6217
Nucleic Acid Atoms
Solvent Atoms	551
Heterogen Atoms	71

Software

Software
Software Name	Purpose
CBASS	data collection
SHELXD	phasing
SHARP	phasing
Coot	model building
CCP4	model building
REFMAC	refinement
HKL-2000	data reduction
HKL-2000	data scaling
CCP4	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.