3LZ8

Structure of a putative chaperone dnaj from klebsiella pneumoniae subsp. pneumoniae mgh 78578 at 2.9 a resolution.

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	9	294	0.1 M Bicine, 10% PEG6000, pH 9.0, VAPOR DIFFUSION, SITTING DROP, temperature 294K

Crystal Properties
Matthews coefficient	Solvent content
1.92	35.81

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 61.886	α = 90
b = 67.396	β = 90
c = 136.818	γ = 90

Symmetry
Space Group	P 21 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	CCD		MIRROR	2010-02-03	M	MOLECULAR REPLACEMENT

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)	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	2.85	68.36	99.7	0.066	0.066	33.848	5.4	13972	13972		-3	97.8

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)
1	2.85	2.9	100		0.733	0.733	2.3	5.5

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	Resolution (High)	Resolution (Low)	Number Reflections (All)	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	3I38	2.9	68.36	13972	13235	654	99.79	0.228	0.226	0.268	RANDOM	68.14

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]
0.78			3.65		-4.44

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	30.564
r_dihedral_angle_3_deg	12.789
r_dihedral_angle_4_deg	12.361
r_scangle_it	4.032
r_dihedral_angle_1_deg	2.594
r_scbond_it	2.385
r_mcangle_it	1.84
r_angle_refined_deg	1.805
r_mcbond_it	0.988
r_angle_other_deg	0.938

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	30.564
r_dihedral_angle_3_deg	12.789
r_dihedral_angle_4_deg	12.361
r_scangle_it	4.032
r_dihedral_angle_1_deg	2.594
r_scbond_it	2.385
r_mcangle_it	1.84
r_angle_refined_deg	1.805
r_mcbond_it	0.988
r_angle_other_deg	0.938
r_mcbond_other	0.155
r_chiral_restr	0.096
r_bond_refined_d	0.014
r_gen_planes_refined	0.008
r_bond_other_d	0.001
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2826
Nucleic Acid Atoms
Solvent Atoms	7
Heterogen Atoms

Software

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

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.