1B67

CRYSTAL STRUCTURE OF THE HISTONE HMFA FROM METHANOTHERMUS FERVIDUS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X31
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X31
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1995-09-15
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	33.720, 52.580, 67.500
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	11.000 - 1.480
R-factor	0.188
R-free	0.26600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	NMR MODEL OF HMFB
RMSD bond length	0.010
RMSD bond angle	0.028
Data reduction software	DENZO
Data scaling software	CCP4 ((AGROVATA)
Phasing software	AMoRE ((CCP4))
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	11.000	1.530
High resolution limit [Å]	1.480	1.480
Rmerge	0.057 *	0.256 *
Total number of observations	77006 *
Number of reflections	20445 *
<I/σ(I)>	2.9	2.9
Completeness [%]	99.1	100
Redundancy	3.8	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	8 *		CRYSTALLISATION IN HANGING DROP RESERVOIR: 2.6 M (NH4)2SO4 PROTEIN WAS MIXED 1 TO 1 WITH RESERVOIR SOLUTION, pH 6.5

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-20 (mg/ml)
2	1	reservoir	potassium citrate	100 (mM)
3	1	reservoir	Tris-HCl	50 (mM)