4EYO

Crystal structure of solute binding protein of ABC transporter from Rhodopseudomonas palustris HaA2 in complex with p-coumaric acid

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	8.5	297	10 mM Nickel chloride, 0.1M Tris, 20% PEG2000 MME, 10 mM Praseodymium Acetate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 297K

Crystal Properties
Matthews coefficient	Solvent content
3.02	59.29

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 88.337	α = 90
b = 88.337	β = 90
c = 210.284	γ = 120

Symmetry
Space Group	P 65 2 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	ADSC QUANTUM 315r		2012-02-02	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 19-ID	0.97929	APS	19-ID

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	1.7	50	99.1	0.113	30.4	6.4	55110	54612		-3

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	1.7	1.71	93.5		0.734	2.12	93.5	1256

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	SAD	THROUGHOUT	1.69	50	54540	54540	2773	99.01	0.1733	0.1733	0.1705	0.2249	RANDOM	29.6055

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]
-1.4	-0.7		-1.4		2.1

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_free	35.46
r_dihedral_angle_2_deg	32.818
r_sphericity_bonded	21.325
r_dihedral_angle_3_deg	14.831
r_dihedral_angle_4_deg	14.376
r_dihedral_angle_1_deg	5.495
r_rigid_bond_restr	5.477
r_angle_refined_deg	1.504
r_chiral_restr	0.103
r_bond_refined_d	0.013

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_free	35.46
r_dihedral_angle_2_deg	32.818
r_sphericity_bonded	21.325
r_dihedral_angle_3_deg	14.831
r_dihedral_angle_4_deg	14.376
r_dihedral_angle_1_deg	5.495
r_rigid_bond_restr	5.477
r_angle_refined_deg	1.504
r_chiral_restr	0.103
r_bond_refined_d	0.013
r_gen_planes_refined	0.007

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2710
Nucleic Acid Atoms
Solvent Atoms	229
Heterogen Atoms	12

Software

Software
Software Name	Purpose
REFMAC	refinement
PDB_EXTRACT	data extraction
SBC-Collect	data collection
HKL-3000	data reduction
HKL-3000	data scaling
HKL-3000	phasing
MLPHARE	phasing
DM	phasing
SHELXDE	phasing
RESOLVE	phasing
ARP/wARP	model building
Coot	model building

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.