2HJS

The structure of a probable aspartate-semialdehyde dehydrogenase from Pseudomonas aeruginosa

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7.4	292	0.2M Ammonium Citrate, 0.1M HEPES pH7.4, 18% PEG 3350, 4% Dioxane, VAPOR DIFFUSION, HANGING DROP, temperature 292K

Crystal Properties
Matthews coefficient	Solvent content
3.7	66.79

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 177.438	α = 90
b = 177.438	β = 90
c = 58.173	γ = 120

Symmetry
Space Group	P 61 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		2005-07-12	M	MAD

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 19-ID	0.97948, 0.97962	APS	19-ID

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (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	2.2	48.6	99.5			26238	26238	-3	-3

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.2	2.28	91.5

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 (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MAD	THROUGHOUT	2.2	48.65	26238	26238	1390	99.58	0.17901	0.17748	0.20888	RANDOM	73.389

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]
0.9	0.45		0.9		-1.35

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.777
r_dihedral_angle_3_deg	16.672
r_dihedral_angle_4_deg	16.158
r_dihedral_angle_1_deg	6.082
r_scangle_it	3.316
r_scbond_it	2.076
r_angle_refined_deg	1.422
r_mcangle_it	1.373
r_mcbond_it	0.85
r_nbtor_refined	0.31

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.777
r_dihedral_angle_3_deg	16.672
r_dihedral_angle_4_deg	16.158
r_dihedral_angle_1_deg	6.082
r_scangle_it	3.316
r_scbond_it	2.076
r_angle_refined_deg	1.422
r_mcangle_it	1.373
r_mcbond_it	0.85
r_nbtor_refined	0.31
r_symmetry_vdw_refined	0.236
r_symmetry_hbond_refined	0.222
r_nbd_refined	0.214
r_xyhbond_nbd_refined	0.177
r_chiral_restr	0.097
r_bond_refined_d	0.013
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2468
Nucleic Acid Atoms
Solvent Atoms	305
Heterogen Atoms	60

Software

Software
Software Name	Purpose
REFMAC	refinement
HKL-3000	phasing
SHELX	phasing
MLPHARE	phasing
DM	phasing
SOLVE	phasing
RESOLVE	phasing
O	model building
Coot	model building
ARP/wARP	model building

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.