3EEH

The crystal structure of the domain of the putative light and redox sensing histidine kinase from Haloarcula marismortui

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP		289	1.0M LiCl, 0.1M NaCl, 30% PEG6000, VAPOR DIFFUSION, SITTING DROP, temperature 289K

Crystal Properties
Matthews coefficient	Solvent content
3.76	67.27

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 96.558	α = 90
b = 96.558	β = 90
c = 40.131	γ = 120

Symmetry
Space Group	P 31 2 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 315	mirrors	2007-10-05	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 19-ID	0.9794	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	1.95	83.62	99.78	0.091	51.9	12.9	15172	15139	2	2	25.2

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	1.95	2	98.45		0.505	3.1	8.4	1165

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 (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	SAD	THROUGHOUT	1.95	83.62	15172	15139	794	99.78	0.18011	0.17907	0.20057	RANDOM	24.035

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	-0.03		-0.07		0.1

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.077
r_dihedral_angle_4_deg	22.607
r_dihedral_angle_3_deg	15.944
r_dihedral_angle_1_deg	6.235
r_scangle_it	4.971
r_scbond_it	3.228
r_mcangle_it	1.974
r_angle_refined_deg	1.835
r_angle_other_deg	1.12
r_mcbond_it	1.017

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.077
r_dihedral_angle_4_deg	22.607
r_dihedral_angle_3_deg	15.944
r_dihedral_angle_1_deg	6.235
r_scangle_it	4.971
r_scbond_it	3.228
r_mcangle_it	1.974
r_angle_refined_deg	1.835
r_angle_other_deg	1.12
r_mcbond_it	1.017
r_mcbond_other	0.258
r_chiral_restr	0.164
r_bond_refined_d	0.019
r_gen_planes_refined	0.006
r_bond_other_d	0.001
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	940
Nucleic Acid Atoms
Solvent Atoms	108
Heterogen Atoms	12

Software

Software
Software Name	Purpose
SBC-Collect	data collection
HKL-3000	phasing
REFMAC	refinement
HKL-3000	data reduction
HKL-3000	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.