1Z9U

Structural Genomics, The crystal structure of the acetyl transferase, modifies N-terminal serine of 50S ribosomal subunit protein L7/L12 from Salmonella typhimurium

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	7	298	2.0M Ammonium sulphate, 0.1M HEPES, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
2.186	41.58

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 86.7	α = 90
b = 86.7	β = 90
c = 237.996	γ = 120

Symmetry
Space Group	P 65 2 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	CCD	SBC-2	mirrors	2004-02-05	M	MAD

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 19-ID	0.9795, 0.9797, 0.94656	APS	19-ID

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	2.2	50	99.58	0.081	32.55	9.1	26396	26286	2	2	48.87

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)
1	2.2	2.28	97.4		0.7	3	7.1	2544

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	MAD	THROUGHOUT	2.2	29.5	26396	26286	1394	99.58	0.21903	0.21903	0.21706	0.25673	RANDOM	48.87

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	0.13		0.25		-0.38

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.019
r_dihedral_angle_4_deg	18.826
r_dihedral_angle_3_deg	15.682
r_dihedral_angle_1_deg	6.065
r_scangle_it	2.293
r_scbond_it	1.529
r_angle_refined_deg	1.215
r_mcangle_it	1.017
r_mcbond_it	0.637
r_nbtor_refined	0.3

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.019
r_dihedral_angle_4_deg	18.826
r_dihedral_angle_3_deg	15.682
r_dihedral_angle_1_deg	6.065
r_scangle_it	2.293
r_scbond_it	1.529
r_angle_refined_deg	1.215
r_mcangle_it	1.017
r_mcbond_it	0.637
r_nbtor_refined	0.3
r_nbd_refined	0.205
r_symmetry_hbond_refined	0.188
r_symmetry_vdw_refined	0.175
r_xyhbond_nbd_refined	0.155
r_chiral_restr	0.094
r_bond_refined_d	0.009
r_gen_planes_refined	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2813
Nucleic Acid Atoms
Solvent Atoms	249
Heterogen Atoms	40

Software

Software
Software Name	Purpose
REFMAC	refinement
SBC-Collect	data collection
HKL-2000	data scaling
CNS	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.