12RH

Structure of turkey hemoglobin A covalently bound with epigallocatechin gallate

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 23-ID-B
Synchrotron site	APS
Beamline	23-ID-B
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-06-14
Detector	DECTRIS EIGER X 16M
Wavelength(s)	1.033202
Spacegroup name	P 21 21 21
Unit cell lengths	80.000, 81.600, 90.520
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	39.580 - 1.995
R-factor	0.1985
Rwork	0.196
R-free	0.23910
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.008
RMSD bond angle	0.846
Data reduction software	XDS (VERSION Jan 10, 2022 BUILT=20220820)
Data scaling software	XSCALE (VERSION Jan 10, 2022 BUILT=20220820)
Phasing software	PHASER
Refinement software	PHENIX (1.21.2_5419)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.310	48.310	2.050
High resolution limit [Å]	1.995	8.940	2.000
Rmerge	0.192	0.060	2.303
Rmeas	0.200	0.063	2.394
Number of reflections	40813	522	2961
<I/σ(I)>	8.84
Completeness [%]	99.9
Redundancy	13.2
CC(1/2)	0.998	0.997	0.811

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		277	THE CONCENTRATION OF HB-EGCG ADDUCT WAS 16 MG/ML IN 10 MM TRIS PH 8.0. THE CRYSTALLIZATION RESERVOIR WAS 20% PEG3350, 0.1 M RACEMIC MALIC ACID, 0.05 M HEPES PH 7.0. 200 NL PROTEIN + 150 NL RESERVOIR. SET BY MOSQUITO IN MRC SD2 PLATES, 50 MICROLITER RESERVOIRS