2GZA

Crystal structure of the VirB11 ATPase from the Brucella Suis type IV secretion system in complex with sulphate

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	8.8	293	16% PEG 4000, 0.1M Tris HCl, 0.2M lithium sulphate, pH 8.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
2.49	50.65

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 118.211	α = 90
b = 125.815	β = 90
c = 164.089	γ = 90

Symmetry
Space Group	C 2 2 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	ADSC QUANTUM 4		2004-07-21	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ESRF BEAMLINE ID14-4	0.97870	ESRF	ID14-4

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	R Sym 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	2.6	29.709	98	0.068	0.068	8.5	7.4	37793	37055	2	2

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.6	2.74	97.5		0.284	0.284	2.7	7.3	5314

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	MOLECULAR REPLACEMENT	THROUGHOUT	PDB entry 1OPX	2.6	29.709	37793	37050	3746	97.73	0.242	0.242	0.238	0.279	RANDOM	40.445

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]
1.64			1.72		-3.36

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	30.442
r_dihedral_angle_4_deg	21.012
r_dihedral_angle_3_deg	18.448
r_dihedral_angle_1_deg	5.056
r_scangle_it	1.497
r_angle_refined_deg	1.479
r_scbond_it	0.847
r_mcangle_it	0.651
r_mcbond_it	0.437
r_nbtor_refined	0.309

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	30.442
r_dihedral_angle_4_deg	21.012
r_dihedral_angle_3_deg	18.448
r_dihedral_angle_1_deg	5.056
r_scangle_it	1.497
r_angle_refined_deg	1.479
r_scbond_it	0.847
r_mcangle_it	0.651
r_mcbond_it	0.437
r_nbtor_refined	0.309
r_symmetry_hbond_refined	0.226
r_nbd_refined	0.205
r_symmetry_vdw_refined	0.2
r_xyhbond_nbd_refined	0.16
r_chiral_restr	0.08
r_bond_refined_d	0.008
r_gen_planes_refined	0.003

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	7569
Nucleic Acid Atoms
Solvent Atoms	193
Heterogen Atoms	15

Software

Software
Software Name	Purpose
EPMR	phasing
ADSC	data collection
CCP4	data scaling
REFMAC	refinement

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.