2AIF

Crystal Structure of High Mobility Like Protein, NHP2, putative from Cryptosporidium parvum

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION	7.5	300	1.5 M Sodium Citrate and 0.1M Hepes pH 7.5, VAPOR DIFFUSION, temperature 300K

Crystal Properties
Matthews coefficient	Solvent content
1.7	27.6

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 90.703	α = 90
b = 90.703	β = 90
c = 31.275	γ = 120

Symmetry
Space Group	H 3

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 4		2005-07-23	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 17-ID	0.97972	APS	17-ID

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	1.895	17.9	90	0.068	0.068	10.7	6.7	6861	6861			25.2

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)
	1.895	1.93	61.3		0.397	0.397	2.01	4	228

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 (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	PDB ENTRY 1E7K	1.895	17.9	6358	6358	499	89.86	0.20335	0.19825	0.27028	RANDOM	39.988

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]
-2.3	-1.15		-2.3		3.44

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.697
r_dihedral_angle_3_deg	22.113
r_dihedral_angle_4_deg	21.825
r_dihedral_angle_1_deg	7.308
r_scangle_it	6.247
r_scbond_it	3.653
r_angle_refined_deg	2.279
r_mcangle_it	2.216
r_mcbond_it	1.346
r_nbtor_refined	0.311

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	40.697
r_dihedral_angle_3_deg	22.113
r_dihedral_angle_4_deg	21.825
r_dihedral_angle_1_deg	7.308
r_scangle_it	6.247
r_scbond_it	3.653
r_angle_refined_deg	2.279
r_mcangle_it	2.216
r_mcbond_it	1.346
r_nbtor_refined	0.311
r_symmetry_vdw_refined	0.262
r_nbd_refined	0.243
r_symmetry_hbond_refined	0.224
r_xyhbond_nbd_refined	0.167
r_chiral_restr	0.16
r_bond_refined_d	0.022
r_gen_planes_refined	0.008

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	870
Nucleic Acid Atoms
Solvent Atoms	30
Heterogen Atoms

Software

Software
Software Name	Purpose
REFMAC	refinement
JDirector	data collection
HKL-2000	data scaling
MOLREP	phasing
O	model building

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.