2QQH

Structure of C8a-MACPF reveals mechanism of membrane attack in complement immune defense

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	8	303	1M LiSO4, 5mM NiCl2, 100mM Tris, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 303K

Crystal Properties
Matthews coefficient	Solvent content
3.98	69.08

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 178.92	α = 90
b = 178.92	β = 90
c = 75.009	γ = 90

Symmetry
Space Group	I 4 2 2

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		2007-03-10	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ESRF BEAMLINE ID29	1.006	ESRF	ID29

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	2.5	40	100	0.08	0.08	17.3	7.1	21349	21349	1	1	63.3

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)
	2.5	2.64	100		0.513	0.513	3.2	7.1	2888

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 (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	SIRAS, MAD	THROUGHOUT	2.5	40	20253	20253	1089	99.98	0.25644	0.25644	0.25475	0.28725	RANDOM	53.487

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]
-0.69			-0.69		1.38

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.78
r_dihedral_angle_4_deg	22.49
r_dihedral_angle_3_deg	18.819
r_dihedral_angle_1_deg	8.501
r_scangle_it	2.405
r_angle_refined_deg	1.703
r_scbond_it	1.621
r_mcangle_it	1.165
r_mcbond_it	0.695
r_nbtor_refined	0.31

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.78
r_dihedral_angle_4_deg	22.49
r_dihedral_angle_3_deg	18.819
r_dihedral_angle_1_deg	8.501
r_scangle_it	2.405
r_angle_refined_deg	1.703
r_scbond_it	1.621
r_mcangle_it	1.165
r_mcbond_it	0.695
r_nbtor_refined	0.31
r_nbd_refined	0.252
r_symmetry_vdw_refined	0.235
r_symmetry_hbond_refined	0.172
r_xyhbond_nbd_refined	0.149
r_chiral_restr	0.125
r_bond_refined_d	0.032
r_gen_planes_refined	0.011

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2402
Nucleic Acid Atoms
Solvent Atoms	44
Heterogen Atoms	16

Software

Software
Software Name	Purpose
REFMAC	refinement
ADSC	data collection
MOSFLM	data reduction
SCALA	data scaling
SOLVE	phasing

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.