12RM

Structure of turkey hemoglobin A at 1.7 Angstrom resolution (tetragonal form)

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	CCD
Collection date	2015-04-12
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97934
Spacegroup name	P 42 21 2
Unit cell lengths	81.310, 81.310, 106.850
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	44.650 - 1.695
R-factor	0.186
Rwork	0.184
R-free	0.21690
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	0.952
Data reduction software	XDS (VERSION Jan 10, 2022 BUILT=20220220)
Data scaling software	XSCALE (VERSION Jan 10, 2022 BUILT=20220220)
Phasing software	PHASER
Refinement software	PHENIX (1.21.2_5419)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	44.650	44.650	1.740
High resolution limit [Å]	1.695	7.580	1.700
Rmerge	0.121	0.043	2.941
Rmeas	0.127	0.046	3.073
Number of reflections	40382	538	2909
<I/σ(I)>	12.79
Completeness [%]	99.9
Redundancy	11.8
CC(1/2)	0.999	0.999	0.440

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	277	200 nL protein at 18.7 mg/mL, 10 mM Tris pH 8.0 was mixed with 200 nL reservoir solution 16 % PEG 3350, 0.2 M sodium citrate. Vapor diffusion in MRC plate. Crystal was cryoprotected by soaking in a solution made by supplementing 16 microliters of reservoir with 2.3 mg solid PEG 3350. Crystals were quenched by looping and direct immersion in liquid nitrogen