3WYQ

Crystal structure of the low-immunogenic core streptavidin mutant LISA-314 (Y22S/Y83S/R84K/E101D/R103K/E116N) at 1.0 A resolution

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	5.2	293	0.2M ammonium sulfate, 0.1M sodium acetate trihydrate, 24% polyethylene glycol 4000, pH 5.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
2.05	39.89

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 63.223	α = 90
b = 67.066	β = 116.68
c = 56.363	γ = 90

Symmetry
Space Group	C 1 2 1

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	RAYONIX MX225HE		2011-10-28	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SPRING-8 BEAMLINE BL44XU	0.82000	SPring-8	BL44XU

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	50	95.4	0.047	30.7		112436	107216

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)
1	1	1.04	91.6		0.296	3.61

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	MOLECULAR REPLACEMENT	THROUGHOUT	1	27.91	101796	5363	95.14	0.13787	0.13654	0.16308	RANDOM	11.191

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	26.74
r_dihedral_angle_4_deg	14.278
r_dihedral_angle_3_deg	12.695
r_dihedral_angle_1_deg	8.571
r_scangle_it	6.695
r_scbond_it	5.265
r_mcangle_it	3.552
r_rigid_bond_restr	2.879
r_mcbond_it	2.587
r_angle_refined_deg	2.426

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	26.74
r_dihedral_angle_4_deg	14.278
r_dihedral_angle_3_deg	12.695
r_dihedral_angle_1_deg	8.571
r_scangle_it	6.695
r_scbond_it	5.265
r_mcangle_it	3.552
r_rigid_bond_restr	2.879
r_mcbond_it	2.587
r_angle_refined_deg	2.426
r_chiral_restr	0.407
r_bond_refined_d	0.026
r_gen_planes_refined	0.012

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1770
Nucleic Acid Atoms
Solvent Atoms	254
Heterogen Atoms	97

Software

Software
Software Name	Purpose
BSS	data collection
PHASER	phasing
REFMAC	refinement
HKL-2000	data reduction
HKL-2000	data scaling

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.