9B1Q

Crystal Structure of human Tryptophan 2,3-dioxygenase in complex with PYN1 inhibitor

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS-II BEAMLINE 17-ID-2
Synchrotron site	NSLS-II
Beamline	17-ID-2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2024-02-10
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.97934
Spacegroup name	P 21 21 2
Unit cell lengths	142.959, 154.170, 88.277
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	34.291 - 2.624
Rwork	0.202
R-free	0.25830
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.417
Data reduction software	autoPROC
Data scaling software	STARANISO
Phasing software	PHASER
Refinement software	REFMAC (5.8.0425)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	34.291	34.291	2.997
High resolution limit [Å]	2.624	8.960	2.624
Rmerge	0.136	0.048	1.060
Rmeas	0.148	0.053	1.142
Rpim	0.058	0.022	0.420
Total number of observations	203088	9063	11616
Number of reflections	31809	1590	1590
<I/σ(I)>	9.62	28.4	1.79
Completeness [%]	93.7	99.1	77.1
Completeness (spherical) [%]	53.8	99.1	8.3
Completeness (ellipsoidal) [%]	93.7	99.1	77.1
Redundancy	6.38	5.7	7.31
CC(1/2)	0.998	0.998	0.647
Anomalous completeness (spherical)	52.4	99.6	7.6
Anomalous completeness	93.4	99.6	76.3
Anomalous redundancy	3.4	3.3	3.9
CC(ano)	-0.177	-0.298	-0.009
|DANO|/σ(DANO)	0.8	0.7	0.8

Diffraction limits	Principal axes of ellipsoid fitted to diffraction cut-off surface
2.608 Å	1.000, 1.000, 1.000
3.336 Å	0.000, 0.000, 0.000
3.666 Å	0.000, 0.000, 0.000
Criteria used in determination of diffraction limits	local <I/sigmaI> ≥ 1.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICROBATCH		298	50 mM Sodium Citrate pH 5.6, 2.0% Tacsimate pH 5.0, 5.0% PEG 3350