2QB3

Structural Studies Reveal the Inactivation of E. coli L-Aspartate Aminotransferase by (s)-4,5-dihydro-2-thiophenecarboxylic acid (SADTA) via Two Mechanisms (at pH 7.5)

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	EVAPORATION	7.5	298	The well solutions contained 25 mM potassium phosphate and 43% saturated ammonium sulfate with 20 mM of SADTA at pH 7.5, EVAPORATION, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
2.94	58.16

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 153.316	α = 90
b = 85.145	β = 90
c = 78.833	γ = 90

Symmetry
Space Group	C 2 2 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	ADSC QUANTUM 315		2005-02-20	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 14-BM-C	0.9	APS	14-BM-C

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	1.45	24.8	97.1	0.056	14.5	6.5		169762

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)
1	1.45	1.5	97.3		0.516	3.6	6.3	8748

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	1.45	24.8	83931	4439	97.14	0.14424	0.14244	0.17774	RANDOM	22.83

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]
-1.24			0.77		0.46

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.251
r_dihedral_angle_4_deg	15.588
r_dihedral_angle_3_deg	13.781
r_dihedral_angle_1_deg	6.048
r_scangle_it	5.719
r_scbond_it	4.245
r_mcangle_it	2.854
r_mcbond_it	2.007
r_angle_refined_deg	1.903
r_nbtor_refined	0.319

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.251
r_dihedral_angle_4_deg	15.588
r_dihedral_angle_3_deg	13.781
r_dihedral_angle_1_deg	6.048
r_scangle_it	5.719
r_scbond_it	4.245
r_mcangle_it	2.854
r_mcbond_it	2.007
r_angle_refined_deg	1.903
r_nbtor_refined	0.319
r_nbd_refined	0.257
r_symmetry_vdw_refined	0.233
r_chiral_restr	0.219
r_xyhbond_nbd_refined	0.194
r_symmetry_hbond_refined	0.186
r_bond_refined_d	0.017
r_gen_planes_refined	0.01

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2978
Nucleic Acid Atoms
Solvent Atoms	414
Heterogen Atoms	92

Software

Software
Software Name	Purpose
REFMAC	refinement
ADSC	data collection
HKL-2000	data reduction
HKL-2000	data scaling
PHASER	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.