2QKW

Structural basis for activation of plant immunity by bacterial effector protein AvrPto

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7.5	293	0.55M potassium sodium tartrate, 0.1M hepes pH 7.5, 10 mM taurine, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
3.21	61.72

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 75.465	α = 90
b = 94.591	β = 90
c = 98.741	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	CCD	MARRESEARCH		2005-03-28	M	MAD
2	1	x-ray	100	IMAGE PLATE	RIGAKU RAXIS IV		2005-03-21	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	BSRF BEAMLINE 3W1A	0.9794, 0.9797, 0.9	BSRF	3W1A
2	ROTATING ANODE	RIGAKU MICROMAX-007	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	3	100	96.2	0.068	20.6		15185	14608	2	1

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)
	3	3.11	88.6		0.67

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 (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MAD	THROUGHOUT	3.2	20	11252	10933	815	97.16	0.27364	0.27364	0.27131	0.30337	RANDOM	96.291

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]
-4.71			3.82		0.89

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.773
r_dihedral_angle_3_deg	18.043
r_dihedral_angle_4_deg	12.924
r_dihedral_angle_1_deg	5.986
r_angle_refined_deg	1.175
r_scangle_it	1.033
r_mcangle_it	0.597
r_scbond_it	0.591
r_mcbond_it	0.334
r_nbtor_refined	0.299

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.773
r_dihedral_angle_3_deg	18.043
r_dihedral_angle_4_deg	12.924
r_dihedral_angle_1_deg	5.986
r_angle_refined_deg	1.175
r_scangle_it	1.033
r_mcangle_it	0.597
r_scbond_it	0.591
r_mcbond_it	0.334
r_nbtor_refined	0.299
r_nbd_refined	0.207
r_symmetry_vdw_refined	0.2
r_symmetry_hbond_refined	0.199
r_xyhbond_nbd_refined	0.147
r_chiral_restr	0.086
r_bond_refined_d	0.008
r_gen_planes_refined	0.003

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3135
Nucleic Acid Atoms
Solvent Atoms
Heterogen Atoms

Software

Software
Software Name	Purpose
REFMAC	refinement
MAR345dtb	data collection
HKL-2000	data reduction
HKL-2000	data scaling
SOLVE	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.