3U7Z

Crystal structure of a putative metal binding protein RUMGNA_00854 (ZP_02040092.1) from Ruminococcus gnavus ATCC 29149 at 1.30 A resolution

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	7.9	293	34.0% polyethylene glycol 400, 0.20M calcium acetate, 0.1M HEPES pH 7.9, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
1.83	32.85

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 29.685	α = 73.13
b = 30.474	β = 83.79
c = 47.156	γ = 89.3

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	MARMOSAIC 325 mm CCD	double crystal monochromator	2011-06-23	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SSRL BEAMLINE BL9-2		SSRL	BL9-2

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (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	1.3	29.504	95	0.067	7.9	2.5	36776	36776

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	1.3	1.33	92.2		0.589	0.589	1.2	2.5	2654

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	PDB entry 2BB6	1.3	29.504	36769	1824	95.03	0.1404	0.1379	0.1887	RANDOM	16.8017

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]
0.02	0.13	-0.09	0.06	-0.14	0.01

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	39.664
r_dihedral_angle_3_deg	11.339
r_sphericity_free	9.434
r_scangle_it	6.877
r_dihedral_angle_1_deg	5.936
r_scbond_it	4.807
r_sphericity_bonded	4.225
r_mcangle_it	3.902
r_mcbond_it	2.731
r_rigid_bond_restr	2.177

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	39.664
r_dihedral_angle_3_deg	11.339
r_sphericity_free	9.434
r_scangle_it	6.877
r_dihedral_angle_1_deg	5.936
r_scbond_it	4.807
r_sphericity_bonded	4.225
r_mcangle_it	3.902
r_mcbond_it	2.731
r_rigid_bond_restr	2.177
r_angle_refined_deg	1.714
r_mcbond_other	1.673
r_angle_other_deg	1.053
r_chiral_restr	0.106
r_bond_refined_d	0.017
r_gen_planes_refined	0.008
r_bond_other_d	0.002
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1504
Nucleic Acid Atoms
Solvent Atoms	167
Heterogen Atoms	44

Software

Software
Software Name	Purpose
MolProbity	model building
PDB_EXTRACT	data extraction
MOLREP	phasing
SCALA	data scaling
REFMAC	refinement
MOSFLM	data reduction

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.