2I0Z

Crystal structure of a FAD binding protein from Bacillus cereus, a putative NAD(FAD)-utilizing dehydrogenases

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	8.3	295	0.01M TRIS-HCL, 0.2M Ammonium chloride, 0.25M Sodium chloride, 20% PEG 3350, pH 8.3, VAPOR DIFFUSION, SITTING DROP, temperature 295K

Crystal Properties
Matthews coefficient	Solvent content
2.15	42.67

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 46.716	α = 90
b = 92.366	β = 90
c = 97.504	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	mirrors	2006-03-06	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 23-ID-D	0.98400	APS	23-ID-D

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	1.84	25	98.9	0.075	13.9	3.9	36967	36967		-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)
	1.84	1.92	99.7		0.394	3.9	3.8	3617

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 (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	PDB ENTRY 2GQF	1.84	24.86	35074	35074	1846	98.87	0.19779	0.19516	0.24794	RANDOM	34.978

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]
0.5			-2.25		1.74

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.967
r_dihedral_angle_4_deg	18.717
r_dihedral_angle_3_deg	14.478
r_dihedral_angle_1_deg	5.598
r_scangle_it	4.222
r_scbond_it	2.801
r_mcangle_it	1.868
r_angle_refined_deg	1.329
r_mcbond_it	1.23
r_nbtor_refined	0.304

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.967
r_dihedral_angle_4_deg	18.717
r_dihedral_angle_3_deg	14.478
r_dihedral_angle_1_deg	5.598
r_scangle_it	4.222
r_scbond_it	2.801
r_mcangle_it	1.868
r_angle_refined_deg	1.329
r_mcbond_it	1.23
r_nbtor_refined	0.304
r_nbd_refined	0.199
r_symmetry_vdw_refined	0.188
r_symmetry_hbond_refined	0.175
r_xyhbond_nbd_refined	0.138
r_chiral_restr	0.094
r_bond_refined_d	0.012
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3282
Nucleic Acid Atoms
Solvent Atoms	380
Heterogen Atoms	54

Software

Software
Software Name	Purpose
REFMAC	refinement
Blu-Ice	data collection
HKL-2000	data reduction
HKL-2000	data scaling
PHASER	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.