3F9I

Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase Rickettsia prowazekii

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	6.2	290	JCSG+ SCREEN D3: 100MM NA/K PO4, 50% PEG 200, 200MM NACL, pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 290K

Crystal Properties
Matthews coefficient	Solvent content
2.35	47.56

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 74.16	α = 90
b = 74.16	β = 90
c = 183.01	γ = 90

Symmetry
Space Group	P 41 21 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	CCD	RIGAKU SATURN 944		2008-11-06	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU MICROMAX-007 HF

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	2.25	19.61	97.9	0.056	20.7			24573		-3	44.7

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	2.25	2.31	93		0.375	2.3

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 (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MR	THROUGHOUT	pdb entry 3emk modified by ccp4 program chainsaw	2.25	19.61	24573	24573	1256	98.1	0.216	0.216	0.213	0.274	RANDOM	30.16

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]
0.2			0.2		-0.4

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.182
r_dihedral_angle_4_deg	18.21
r_dihedral_angle_3_deg	16.264
r_dihedral_angle_1_deg	6.692
r_scangle_it	3.469
r_scbond_it	2.123
r_angle_refined_deg	1.6
r_mcangle_it	1.571
r_angle_other_deg	0.939
r_mcbond_it	0.853

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.182
r_dihedral_angle_4_deg	18.21
r_dihedral_angle_3_deg	16.264
r_dihedral_angle_1_deg	6.692
r_scangle_it	3.469
r_scbond_it	2.123
r_angle_refined_deg	1.6
r_mcangle_it	1.571
r_angle_other_deg	0.939
r_mcbond_it	0.853
r_mcbond_other	0.234
r_chiral_restr	0.085
r_bond_refined_d	0.017
r_gen_planes_refined	0.005
r_bond_other_d	0.003
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3252
Nucleic Acid Atoms
Solvent Atoms	129
Heterogen Atoms

Software

Software
Software Name	Purpose
StructureStudio	data collection
PHASER	phasing
REFMAC	refinement
XDS	data reduction
XSCALE	data scaling

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.