4QHW

Crystal structure of a putative two-domain sugar hydrolase (BACCAC_02064) from Bacteroides caccae ATCC 43185 at 1.35 A resolution

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	7.5	277	2.0M ammonium sulfate, 2.0% polyethylene glycol 400, 0.1M sodium HEPES pH 7.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
3.17	61.23

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 87.055	�� = 90
b = 117.803	�� = 90
c = 113.748	�� = 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 325 mm CCD	Vertical focusing mirror; double crystal Si(111) monochromator	2014-04-16	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SSRL BEAMLINE BL14-1		SSRL	BL14-1

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	1.35	29.812	99.8	0.11	8.2	5.7	127336	127336

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)
1	1.35	1.39	97.4		0.501	0.501	1.5	2.6	8830

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	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	1.35	29.812	127307	6399	99.72	0.1074	0.106	0.1336	RANDOM	20.6094

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]
-0.29			0.08		0.21

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.285
r_sphericity_free	31.118
r_dihedral_angle_4_deg	23.349
r_sphericity_bonded	13.206
r_dihedral_angle_3_deg	11.167
r_dihedral_angle_1_deg	6.703
r_rigid_bond_restr	6.354
r_angle_refined_deg	2.263
r_mcangle_it	2.172
r_mcbond_it	1.914

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.285
r_sphericity_free	31.118
r_dihedral_angle_4_deg	23.349
r_sphericity_bonded	13.206
r_dihedral_angle_3_deg	11.167
r_dihedral_angle_1_deg	6.703
r_rigid_bond_restr	6.354
r_angle_refined_deg	2.263
r_mcangle_it	2.172
r_mcbond_it	1.914
r_mcbond_other	1.861
r_angle_other_deg	1.121
r_chiral_restr	0.134
r_bond_refined_d	0.026
r_gen_planes_refined	0.012
r_gen_planes_other	0.004
r_bond_other_d	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3230
Nucleic Acid Atoms
Solvent Atoms	690
Heterogen Atoms	88

Software

Software
Software Name	Purpose
MolProbity	model building
PDB_EXTRACT	data extraction
SHELX	phasing
SHARP	phasing
SCALA	data scaling
REFMAC	refinement
MOSFLM	data reduction
SHELXD	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 R01GM157729.