4QVS

2.1 Angstrom resolution crystal structure of S-layer domain-containing protein (residues 221-444) from Clostridium thermocellum ATCC 27405

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	8.5	295	protein: 9.35 mg/mL in 10 mM Tris-HCl pH 8.3, 500 mM NaCl, 5 mM BME, crystallization: The PEGs II Suite G11 (83): 0.5 M Lithium chloride, 0.1 M Tris pH 8.5. 28% (w/v) PEG 6000, cyo: well solution, VAPOR DIFFUSION, SITTING DROP, temperature 295K

Crystal Properties
Matthews coefficient	Solvent content
2.21	44.3

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 65.958	α = 90
b = 74.813	β = 90
c = 98.398	γ = 90

Symmetry
Space Group	C 2 2 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	MARMOSAIC 225 mm CCD	Beryllium lenses	2014-06-04	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 21-ID-F	0.97872	APS	21-ID-F

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	2.1	30	99.1	0.079	43.56	7	14480	14480		-3	48.6

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	2.1	2.14	95.3		0.62	2.6	6.2	668

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	2.1	27.35	13697	13697	721	99.01	0.20994	0.20802	0.24878	RANDOM	61.661

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]
-5.6			-0.74		6.34

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	30.246
r_dihedral_angle_4_deg	14.1
r_dihedral_angle_3_deg	10.693
r_dihedral_angle_1_deg	4.326
r_angle_refined_deg	1.814
r_angle_other_deg	0.833
r_chiral_restr	0.109
r_bond_refined_d	0.013
r_gen_planes_refined	0.007
r_bond_other_d	0.001

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	30.246
r_dihedral_angle_4_deg	14.1
r_dihedral_angle_3_deg	10.693
r_dihedral_angle_1_deg	4.326
r_angle_refined_deg	1.814
r_angle_other_deg	0.833
r_chiral_restr	0.109
r_bond_refined_d	0.013
r_gen_planes_refined	0.007
r_bond_other_d	0.001
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1673
Nucleic Acid Atoms
Solvent Atoms	44
Heterogen Atoms	2

Software

Software
Software Name	Purpose
Blu-Ice	data collection
PHENIX	model building
REFMAC	refinement
xia2	data reduction
MOSFLM	data reduction
pointless	data scaling
Aimless	data scaling
xia2	data scaling
PHENIX	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.