Experiment: 2PH7

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	Modified Microbatch	4.9	291	USING 1.0 MICROLITER DROPS CONTAINING EQUAL VOLUMES OF PROTEIN CONCENTRATE (12 mg/mL) AND SOLUTION CONTAINING 20% PEG 4000, 0.05M SODIUM CHLORIDE, 0.05M LITHIUM SULFATE, 0.1M SODIUM ACETATE pH 4.9, Modified Microbatch, temperature 291K

Crystal Properties
Matthews coefficient	Solvent content
3.17	61.16

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 206.536	α = 90
b = 206.536	β = 90
c = 206.536	γ = 90

Symmetry
Space Group	F 2 3

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	ROSENBAUM	2007-01-31	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 22-ID	0.97240	APS	22-ID

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	2.4	47.4	99.9	0.066	39.3	6.7		28734

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
	2.4	2.49	99.8		0.535	2.08	5.2	2858

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Cut-off Sigma (F)	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	2.4	47.4	2	27283	27283	1423	99.9	0.23225	0.23022	0.27143	RANDOM	47.574

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]

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	30.582
r_dihedral_angle_3_deg	16.644
r_dihedral_angle_4_deg	15.547
r_dihedral_angle_1_deg	10.231
r_scangle_it	2.881
r_scbond_it	1.84
r_mcangle_it	1.372
r_angle_refined_deg	1.341
r_mcbond_it	1.172
r_nbtor_refined	0.306

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	30.582
r_dihedral_angle_3_deg	16.644
r_dihedral_angle_4_deg	15.547
r_dihedral_angle_1_deg	10.231
r_scangle_it	2.881
r_scbond_it	1.84
r_mcangle_it	1.372
r_angle_refined_deg	1.341
r_mcbond_it	1.172
r_nbtor_refined	0.306
r_chiral_restr	0.234
r_nbd_refined	0.201
r_symmetry_vdw_refined	0.183
r_xyhbond_nbd_refined	0.151
r_symmetry_hbond_refined	0.141
r_bond_refined_d	0.01
r_gen_planes_refined	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3583
Nucleic Acid Atoms
Solvent Atoms	72
Heterogen Atoms

Software

Software
Software Name	Purpose
REFMAC	refinement
SERGUI	data collection
HKL-2000	data reduction
HKL-2000	data scaling
SGXPRO	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.