1DXC

CO complex of Myoglobin Mb-YQR at 100K

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12C
Synchrotron site	NSLS
Beamline	X12C
Temperature [K]	100
Detector technology	CCD
Collection date	1998-05-15
Detector	PRINCETON SCIENTIFIC
Spacegroup name	P 6
Unit cell lengths	90.610, 90.610, 45.330
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	19.600 - 1.400
R-factor	0.129 *
Rwork	0.128
R-free	0.15300 *
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.014
RMSD bond angle	2.545
Data reduction software	XDS
Data scaling software	XSCALE
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.600	1.500
High resolution limit [Å]	1.400	1.400
Rmerge	0.036 *	0.125 *
Total number of observations	143218 *
Number of reflections	40518	7138 *
<I/σ(I)>	19.8	3.6
Completeness [%]	96.5	91.4
Redundancy	3.5	2.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	8.7 *	21 *	PROTEIN WAS CRYSTALLIZED FROM 3.6 M AMMONIUM SULFATE.CRYSTALS WERE SOAKED FOR C.A. 1 HOUR IN A THOROUGHLY DEGASSED AND CO SATURATED CRYOPROTECTANT SOLUTION MADE BY ADDITION OF 100 MG XYLITOL, 100 MG GLUCOSE AND 8 MG NA-DITHIONATE TO 1 ML OF 70% SATURATED AMMONIUM SULFATE WITH 50 MM TRIS.HCL PH 9.0. DISTINCT COLOR CHANGES INDICATED THE FORMATION OF CO-MB FROM MET-MB.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	1 (mM)
2	1	reservoir	ammonium sulfate	2.7 (M)
3	1	reservoir	Tris-HCl	20 (mM)
4	1	reservoir	EDTA	1 (mM)