1S3I

Crystal structure of the N terminal hydrolase domain of 10-formyltetrahydrofolate dehydrogenase

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	5	277	1.3 M ammonium sulphate, 0.1M sodium acetate pH 5.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
3.11	60.09

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 100	α = 90
b = 64.63	β = 90
c = 64.59	γ = 90

Symmetry
Space Group	P 21 21 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	IMAGE PLATE	RIGAKU RAXIS IV	mirrors	2001-12-02	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU RU300	1.54

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	2.3	45.7	99.7	0.1	0.1	5.3	4.2	19201	19201			32.9

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)
	2.3	2.38	100		0.346	0.346	2	4.2	1863

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 (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MIR	THROUGHOUT	2.3	15	19056	19056	978	100	0.2453	0.24532	0.24205	0.30527	RANDOM	33.745

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]
-0.72			0.01		0.71

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_1_deg	7.637
r_scangle_it	2.576
r_scbond_it	1.658
r_angle_refined_deg	1.481
r_mcangle_it	1.107
r_mcbond_it	0.577
r_nbd_refined	0.207
r_symmetry_vdw_refined	0.176
r_symmetry_hbond_refined	0.134
r_xyhbond_nbd_refined	0.13

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_1_deg	7.637
r_scangle_it	2.576
r_scbond_it	1.658
r_angle_refined_deg	1.481
r_mcangle_it	1.107
r_mcbond_it	0.577
r_nbd_refined	0.207
r_symmetry_vdw_refined	0.176
r_symmetry_hbond_refined	0.134
r_xyhbond_nbd_refined	0.13
r_chiral_restr	0.118
r_bond_refined_d	0.01
r_gen_planes_refined	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2380
Nucleic Acid Atoms
Solvent Atoms	53
Heterogen Atoms	20

Software

Software
Software Name	Purpose
REFMAC	refinement
CrystalClear	data reduction
d*TREK	data scaling
PHASES	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.