4WY9

Crystal structure of the periplasmic sensory domain of the Campylobacter jejuni chemoreceptor Tlp1

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	5.5	293	200 mM ammonium acetate, 23%(w/v) PEG 3350 and 100 mM Bis-Tris pH 5.5

Crystal Properties
Matthews coefficient	Solvent content
2.19	43.94

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 39.26	α = 92.52
b = 43.32	β = 111.38
c = 50.9	γ = 114.73

Symmetry
Space Group	P 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 315r		2014-09-27	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	AUSTRALIAN SYNCHROTRON BEAMLINE MX1	1.0	Australian Synchrotron	MX1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	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	1.4	38.27	91.5	0.031	0.031	0.998	11.9	2		49677

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Rpim I (All)	CC (Half)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.4	1.42	66.2		0.149	0.149	0.944	3.9	2	1741

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	TlpC	1.4	15	47127	2535	91.43	0.1187	0.1169	0.1542	RANDOM	17.065

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]
-0.07	-0.02	-0.1	0.17	-0.03	-0.01

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.634
r_sphericity_free	32.028
r_dihedral_angle_3_deg	12.625
r_sphericity_bonded	10.37
r_rigid_bond_restr	10.277
r_dihedral_angle_4_deg	7.967
r_dihedral_angle_1_deg	5.836
r_angle_other_deg	2.955
r_mcangle_it	2.293
r_mcbond_it	1.867

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.634
r_sphericity_free	32.028
r_dihedral_angle_3_deg	12.625
r_sphericity_bonded	10.37
r_rigid_bond_restr	10.277
r_dihedral_angle_4_deg	7.967
r_dihedral_angle_1_deg	5.836
r_angle_other_deg	2.955
r_mcangle_it	2.293
r_mcbond_it	1.867
r_mcbond_other	1.862
r_angle_refined_deg	1.308
r_chiral_restr	0.08
r_bond_refined_d	0.014
r_gen_planes_other	0.009
r_gen_planes_refined	0.007
r_bond_other_d

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2247
Nucleic Acid Atoms
Solvent Atoms	414
Heterogen Atoms	5

Software

Software
Software Name	Purpose
Aimless	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
PHASER	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.