3QRH

Crystal structure of fructose bisphosphate aldolase from Encephalitozoon Cuniculi, bound to glyceraldehyde 3-phosphate

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	7	290	10% PEG6000, 0.1 M HEPES, protein at ~22 mg/ml, glyceraldehyde 3-phosphate at 10 mM., pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 290K

Crystal Properties
Matthews coefficient	Solvent content
3.47	64.57

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 122.54	α = 90
b = 138.09	β = 90
c = 62.8	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		2011-02-10	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ALS BEAMLINE 5.0.1	0.977400	ALS	5.0.1

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	2	50	99.8	0.052	22.64	6	36410	36353		-3	35.215

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)
	2	2.05	100		0.438	4.2	6.1	2650

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	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	pdb entry 3MBF	2	46.46	36267	1783	99.63	0.164	0.163	0.187	RANDOM	30.407

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]
-1.26			-0.5		1.77

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.463
r_dihedral_angle_4_deg	17.117
r_dihedral_angle_3_deg	13.279
r_dihedral_angle_1_deg	5.772
r_scangle_it	3.482
r_scbond_it	2.186
r_angle_refined_deg	1.395
r_mcangle_it	1.343
r_angle_other_deg	0.919
r_mcbond_it	0.764

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.463
r_dihedral_angle_4_deg	17.117
r_dihedral_angle_3_deg	13.279
r_dihedral_angle_1_deg	5.772
r_scangle_it	3.482
r_scbond_it	2.186
r_angle_refined_deg	1.395
r_mcangle_it	1.343
r_angle_other_deg	0.919
r_mcbond_it	0.764
r_mcbond_other	0.224
r_chiral_restr	0.087
r_bond_refined_d	0.016
r_gen_planes_refined	0.006
r_bond_other_d	0.001
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2591
Nucleic Acid Atoms
Solvent Atoms	221
Heterogen Atoms	9

Software

Software
Software Name	Purpose
XSCALE	data scaling
PHASER	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
ADSC	data collection
XDS	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.