1U0G

Crystal structure of mouse phosphoglucose isomerase in complex with erythrose 4-phosphate

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	8.5	294	1.9 M ammonium sulphate, 100 mM Tris-HCl, pH 8.5 , VAPOR DIFFUSION, HANGING DROP, temperature 294K

Crystal Properties
Matthews coefficient	Solvent content
2.3	41.5

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 68.8	α = 90
b = 115.6	β = 100.2
c = 73.2	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	IMAGE PLATE	RIGAKU RAXIS IV	mirrors	2002-04-10	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	1.7	54	97.5	0.067	0.067	7.4	4.2	123637	123637			19.3

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	1.7	1.76	81.8		0.271	0.271	1.9	3	12331

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 (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	REFINEMENT	THROUGHOUT	NATIVE STRUCTURE	1.7	50	118864	118664	5943	97.5	0.192	0.192	0.19	0.215	RANDOM	19.099

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]
-0.25		-0.35	-0.37		0.49

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_1_deg	5.421
r_scangle_it	2.177
r_scbond_it	1.325
r_angle_refined_deg	1.052
r_mcangle_it	0.757
r_mcbond_it	0.396
r_nbd_refined	0.19
r_symmetry_vdw_refined	0.163
r_xyhbond_nbd_refined	0.119
r_symmetry_hbond_refined	0.105

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_1_deg	5.421
r_scangle_it	2.177
r_scbond_it	1.325
r_angle_refined_deg	1.052
r_mcangle_it	0.757
r_mcbond_it	0.396
r_nbd_refined	0.19
r_symmetry_vdw_refined	0.163
r_xyhbond_nbd_refined	0.119
r_symmetry_hbond_refined	0.105
r_chiral_restr	0.08
r_bond_refined_d	0.008
r_gen_planes_refined	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	8814
Nucleic Acid Atoms
Solvent Atoms	832
Heterogen Atoms	115

Software

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

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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.