3P96

Crystal structure of Phosphoserine phosphatase SerB from Mycobacterium avium, native form

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	6	290	0.2 M MgCl2, 0.1 M MES, 20% PEG6000, protein at 27.45mg/ml, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 290K

Crystal Properties
Matthews coefficient	Solvent content
2.6	52.69

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 65.53	α = 90
b = 109.19	β = 90
c = 134.32	γ = 90

Symmetry
Space Group	I 2 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	ADSC QUANTUM 315		2010-09-15	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ALS BEAMLINE 5.0.1	0.9774	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	2.05	36.97	96.5	0.062	16.41	5.7	30644	29584		-3	38.011

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	2.05	2.1	85.8		0.554	3.7	4.3	2232

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	SAD	THROUGHOUT	2.05	36.97	30644	29505	1493	96.31	0.231	0.231	0.229	0.281	RANDOM	45.015

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]
3.27			-0.53		-2.73

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.149
r_dihedral_angle_4_deg	19.613
r_dihedral_angle_3_deg	14.31
r_dihedral_angle_1_deg	6.583
r_scangle_it	3.385
r_scbond_it	2.131
r_angle_refined_deg	1.54
r_mcangle_it	1.301
r_angle_other_deg	0.948
r_mcbond_it	0.722

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.149
r_dihedral_angle_4_deg	19.613
r_dihedral_angle_3_deg	14.31
r_dihedral_angle_1_deg	6.583
r_scangle_it	3.385
r_scbond_it	2.131
r_angle_refined_deg	1.54
r_mcangle_it	1.301
r_angle_other_deg	0.948
r_mcbond_it	0.722
r_mcbond_other	0.167
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	2890
Nucleic Acid Atoms
Solvent Atoms	112
Heterogen Atoms	6

Software

Software
Software Name	Purpose
XSCALE	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
ADSC	data collection
XDS	data reduction
PHENIX	phasing

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 R01GM157729.