2APG

The structure of tryptophan 7-halogenase (PrnA)suggests a mechanism for regioselective chlorination

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	8		10% PEG8000, 0.1M imidazole pH8.0, 0.2M Ca(CH3CO2)2, VAPOR DIFFUSION, SITTING DROP, temperature 100K

Crystal Properties
Matthews coefficient	Solvent content
2.6	52.4

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 67.52	�� = 90
b = 67.52	�� = 90
c = 275.019	�� = 90

Symmetry
Space Group	P 43 21 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 4	mirrors	2003-10-04	M	MAD

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	BESSY BEAMLINE 14.2	0.933	BESSY	14.2

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	1.9	69.01	98	0.132	0.113	3.8	3.8	66245	48481	7.8	3	23.988

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	1.9	1.949	99.5		0.564	0.484	1	3.7	3759

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Cut-off Sigma (I)	Cut-off Sigma (F)	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	1.9	69.01	3	7.8	51779	48481	2610	99.2	0.1781	0.175	0.17631	0.211	RANDOM	24.407

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]
0.77			0.77		-1.54

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	32.281
r_dihedral_angle_4_deg	17.904
r_dihedral_angle_3_deg	13.43
r_dihedral_angle_1_deg	6.131
r_scangle_it	3.518
r_scbond_it	2.336
r_angle_refined_deg	1.544
r_mcangle_it	1.434
r_mcbond_it	0.959
r_nbtor_refined	0.316

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	32.281
r_dihedral_angle_4_deg	17.904
r_dihedral_angle_3_deg	13.43
r_dihedral_angle_1_deg	6.131
r_scangle_it	3.518
r_scbond_it	2.336
r_angle_refined_deg	1.544
r_mcangle_it	1.434
r_mcbond_it	0.959
r_nbtor_refined	0.316
r_nbd_refined	0.214
r_symmetry_hbond_refined	0.192
r_symmetry_vdw_refined	0.169
r_xyhbond_nbd_refined	0.156
r_chiral_restr	0.1
r_bond_refined_d	0.015
r_gen_planes_refined	0.007

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	4162
Nucleic Acid Atoms
Solvent Atoms	404
Heterogen Atoms	59

Software

Software
Software Name	Purpose
REFMAC	refinement
MOSFLM	data reduction
CCP4	data scaling
SOLVE	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.