2AO9

Structural Genomics, The crystal structure of a Phage protein (phBC6A51) from Bacillus cereus ATCC 14579

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	9.5	298	1.26M (NH)4SO4, 0.1M CHES. 0.2M NaCl, pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
2.67	53

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 114.016	α = 90
b = 150.481	β = 90
c = 99.975	γ = 90

Symmetry
Space Group	P 21 21 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	SBC-3	mirrors	2004-10-28	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 19-ID	0.9798	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	1.9	50	99.6	0.09	22.76	4.9	135664	134863	2	2	30.4

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	1.9	1.97	99.1		0.61	2	4.8	25899

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	1.9	39.1	128540	128090	6772	99.65	0.2065	0.2065	0.20494	0.23581	RANDOM	30.437

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]
1.43			-0.72		-0.7

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.969
r_dihedral_angle_4_deg	17.758
r_dihedral_angle_3_deg	15.683
r_dihedral_angle_1_deg	5.12
r_scangle_it	3.22
r_scbond_it	2.144
r_mcangle_it	1.326
r_angle_refined_deg	1.072
r_mcbond_it	0.826
r_nbtor_refined	0.294

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.969
r_dihedral_angle_4_deg	17.758
r_dihedral_angle_3_deg	15.683
r_dihedral_angle_1_deg	5.12
r_scangle_it	3.22
r_scbond_it	2.144
r_mcangle_it	1.326
r_angle_refined_deg	1.072
r_mcbond_it	0.826
r_nbtor_refined	0.294
r_symmetry_vdw_refined	0.239
r_nbd_refined	0.199
r_xyhbond_nbd_refined	0.196
r_symmetry_hbond_refined	0.146
r_chiral_restr	0.073
r_bond_refined_d	0.011
r_gen_planes_refined	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	8172
Nucleic Acid Atoms
Solvent Atoms	971
Heterogen Atoms

Software

Software
Software Name	Purpose
REFMAC	refinement
SBC-Collect	data collection
HKL-2000	data scaling
CNS	phasing

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.