4KLX

Crystal structure of dihydrofolate reductase from Mycobacterium tuberculosis in an open conformation.

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7	298	8% PEG 4000, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
1.98	37.81

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 32.41	α = 90
b = 63.06	β = 100.82
c = 78.16	γ = 90

Symmetry
Space Group	P 1 21 1

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 1		2010-11-04	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ESRF BEAMLINE ID14-1	0.93340	ESRF	ID14-1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (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	1.23	76.77	99.3	0.107	7	3.3	88928	88928	2	2

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	1.23	1.3	97.9		0.474	0.474	1.6	3.2	12800

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	MOLECULAR REPLACEMENT	THROUGHOUT	1.23	19.87	88928	88844	4452	99.14	0.1835	0.1804	0.2438	RANDOM	12.3997

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]

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_free	33.084
r_dihedral_angle_2_deg	30.521
r_dihedral_angle_4_deg	16.6
r_dihedral_angle_3_deg	12.288
r_sphericity_bonded	11.279
r_dihedral_angle_1_deg	7.125
r_rigid_bond_restr	6.992
r_angle_refined_deg	2.48
r_chiral_restr	0.273
r_bond_refined_d	0.025

RMS Deviations
Key	Refinement Restraint Deviation
r_sphericity_free	33.084
r_dihedral_angle_2_deg	30.521
r_dihedral_angle_4_deg	16.6
r_dihedral_angle_3_deg	12.288
r_sphericity_bonded	11.279
r_dihedral_angle_1_deg	7.125
r_rigid_bond_restr	6.992
r_angle_refined_deg	2.48
r_chiral_restr	0.273
r_bond_refined_d	0.025
r_gen_planes_refined	0.017

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2497
Nucleic Acid Atoms
Solvent Atoms	523
Heterogen Atoms	76

Software

Software
Software Name	Purpose
SCALA	data scaling
PHASER	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
ADSC	data collection
MOSFLM	data reduction

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.