3M9H

Crystal structure of the amino terminal coiled coil domain of the Mycobacterium tuberculosis proteasomal ATPase Mpa

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	5.5	293	0.1M sodium citrate, 2.1M ammonium sulfate, 0.24M sodium/potassium tartrate 0.25M sodium chloride, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
1.76	30.1

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 80.752	α = 90
b = 114.164	β = 90
c = 114.49	γ = 90

Symmetry
Space Group	F 2 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 315r		2010-01-30	M	SINGLE WAVELENGTH
2	1	x-ray	100	CCD	ADSC QUANTUM 315		2010-01-22	M	SINGLE WAVELENGTH
3	1	x-ray	100	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	NSLS BEAMLINE X25	0.9795	NSLS	X25
2	SYNCHROTRON	NSLS BEAMLINE X29A	0.9193	NSLS	X29A
3	SYNCHROTRON	NSLS BEAMLINE X29A	1.0809	NSLS	X29A

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
1,2,3	2	25	99	0.085		14.5	18001	17050		2

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)
	2	2.03	99		0.541			890

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	2	25	17050	921	98.95	0.209	0.206	0.274	RANDOM	38.744

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]
-0.16			0.25		-0.09

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.266
r_dihedral_angle_4_deg	22.468
r_dihedral_angle_3_deg	18.79
r_scangle_it	10.047
r_scbond_it	5.993
r_dihedral_angle_1_deg	5.034
r_mcangle_it	4.357
r_rigid_bond_restr	3.325
r_mcbond_it	2.434
r_angle_refined_deg	1.842

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.266
r_dihedral_angle_4_deg	22.468
r_dihedral_angle_3_deg	18.79
r_scangle_it	10.047
r_scbond_it	5.993
r_dihedral_angle_1_deg	5.034
r_mcangle_it	4.357
r_rigid_bond_restr	3.325
r_mcbond_it	2.434
r_angle_refined_deg	1.842
r_chiral_restr	0.111
r_bond_refined_d	0.023
r_gen_planes_refined	0.007

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2088
Nucleic Acid Atoms
Solvent Atoms	60
Heterogen Atoms

Software

Software
Software Name	Purpose
REFMAC	refinement
PDB_EXTRACT	data extraction
HKL-2000	data collection
HKL-2000	data reduction
HKL-2000	data scaling
PHENIX	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.