Experiment: 4RWC

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	6.5	298	Racemic M2-TM dissolved at ~3 mg/mL in 2% solution (w/v) racemic OG. Hanging drops of 1 uL peptide stock combined with 1 uL of precipitant containing 0.1 M ADA pH 6.5, 1.0 M ammonium sulfate were equilibrated with 500 uL reservoir volumes of precipitant., VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
2.1	41.39

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 15.35	α = 90.01
b = 25.88	β = 99.49
c = 26.97	γ = 99.91

Symmetry
Space Group	P -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	MARMOSAIC 225 mm CCD		2014-06-09	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	1.05	26.59	92.6	0.072	12.89	6.01		17458			5.3

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	1.05	1.08	65.9		0.381	2.54	2.54

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	1.05	26.59	17310	867	91.83	0.1392	0.1383	0.1556	RANDOM	14.015

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]
-0.25	0.49	-0.35	0.67	1.36	-0.53

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_free	29.373
r_sphericity_bonded	20.614
r_dihedral_angle_2_deg	16.953
r_dihedral_angle_3_deg	12.27
r_dihedral_angle_1_deg	3.961
r_rigid_bond_restr	2.09
r_angle_refined_deg	1.551
r_dihedral_angle_4_deg	1.048
r_angle_other_deg	0.751
r_chiral_restr	0.08

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_free	29.373
r_sphericity_bonded	20.614
r_dihedral_angle_2_deg	16.953
r_dihedral_angle_3_deg	12.27
r_dihedral_angle_1_deg	3.961
r_rigid_bond_restr	2.09
r_angle_refined_deg	1.551
r_dihedral_angle_4_deg	1.048
r_angle_other_deg	0.751
r_chiral_restr	0.08
r_bond_refined_d	0.01
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	177
Nucleic Acid Atoms
Solvent Atoms	28
Heterogen Atoms	36

Software

Software
Software Name	Purpose
XPREP	data reduction
REFMAC	refinement
PDB_EXTRACT	data extraction
EMBL	data collection
XDS	data reduction
XSCALE	data scaling
PHASER	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.