2Q5E

Crystal structure of human carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 2

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION	7	294	2.8 M Sodium acetate, pH 7.0, VAPOR DIFFUSION, temperature 294K

Crystal Properties
Matthews coefficient	Solvent content
3.2	61.53

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 108.643	α = 90
b = 117.637	β = 90
c = 170.134	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	ADSC QUANTUM 315		2007-04-28	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 31-ID	0.97958	APS	31-ID

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (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	2.51	96.76	96.5	0.072	0.072	18.6	5.1	72419	72419			56.1

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)
	2.51	2.65	81.7		0.447	0.447	2.6	3.6	8821

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	2.51	20	72246	72246	3629	96.38	0.219	0.216	0.278	RANDOM	45.075

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]
-0.51			-0.06		0.57

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.309
r_dihedral_angle_4_deg	23.685
r_dihedral_angle_3_deg	20.709
r_dihedral_angle_1_deg	7.28
r_scangle_it	4.716
r_scbond_it	3.067
r_angle_refined_deg	2.084
r_mcangle_it	2.059
r_mcbond_it	1.225
r_symmetry_hbond_refined	0.382

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.309
r_dihedral_angle_4_deg	23.685
r_dihedral_angle_3_deg	20.709
r_dihedral_angle_1_deg	7.28
r_scangle_it	4.716
r_scbond_it	3.067
r_angle_refined_deg	2.084
r_mcangle_it	2.059
r_mcbond_it	1.225
r_symmetry_hbond_refined	0.382
r_nbtor_refined	0.33
r_nbd_refined	0.243
r_xyhbond_nbd_refined	0.211
r_symmetry_vdw_refined	0.199
r_chiral_restr	0.141
r_bond_refined_d	0.022
r_metal_ion_refined	0.022
r_gen_planes_refined	0.008

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	11467
Nucleic Acid Atoms
Solvent Atoms	91
Heterogen Atoms	8

Software

Software
Software Name	Purpose
SCALA	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
CBASS	data collection
DENZO	data reduction
SHELXCD	phasing
SHELXE	model building

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.