6ET6

Crystal structure of muramidase from Acinetobacter baumannii AB 5075UW prophage

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION		293	0.2M Li2SO4; 0.1M MES pH 6.5; 25% PEG3350

Crystal Properties
Matthews coefficient	Solvent content
1.82	32.32

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 30.98	α = 90
b = 67	β = 90
c = 75.76	γ = 90

Symmetry
Space Group	P 2 21 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	PIXEL	DECTRIS PILATUS 6M-F		2017-07-01	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SPRING-8 BEAMLINE BL41XU	0.8	SPring-8	BL41XU

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	Rpim I (All)	CC (Half)	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	1.2	50.18	94.1	0.113	0.126	0.054	0.994	5.6	5		46812

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	Rpim I (All)	CC (Half)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.2	1.22	94.6		0.929	1.039	0.452	0.762		5

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	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	2ANV	1.2	50.18	44084	2373	92.52	0.1485	0.1474	0.1685	RANDOM	17.417

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]
-0.51			1.19		-0.68

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_free	32.476
r_dihedral_angle_2_deg	31.418
r_dihedral_angle_4_deg	12.027
r_dihedral_angle_3_deg	11.037
r_sphericity_bonded	9.976
r_dihedral_angle_1_deg	5.574
r_rigid_bond_restr	3.195
r_angle_other_deg	2.118
r_angle_refined_deg	1.901
r_chiral_restr	0.14

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_free	32.476
r_dihedral_angle_2_deg	31.418
r_dihedral_angle_4_deg	12.027
r_dihedral_angle_3_deg	11.037
r_sphericity_bonded	9.976
r_dihedral_angle_1_deg	5.574
r_rigid_bond_restr	3.195
r_angle_other_deg	2.118
r_angle_refined_deg	1.901
r_chiral_restr	0.14
r_bond_refined_d	0.019
r_gen_planes_refined	0.01
r_bond_other_d	0.002
r_gen_planes_other	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1139
Nucleic Acid Atoms
Solvent Atoms	229
Heterogen Atoms	11

Software

Software
Software Name	Purpose
HKL-2000	data collection
Aimless	data scaling
MoRDa	model building
REFMAC	refinement
PDB_EXTRACT	data extraction
MOSFLM	data reduction
MOLREP	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.