1BR8

IMPLICATIONS FOR FUNCTION AND THERAPY OF A 2.9A STRUCTURE OF BINARY-COMPLEXED ANTITHROMBIN

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX7.2
Synchrotron site	SRS
Beamline	PX7.2
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-08-15
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	69.120, 101.690, 87.020
Unit cell angles	90.00, 104.36, 90.00

Refinement procedure

Resolution	6.000 - 2.900
R-factor	0.228 *
R-free	0.29700 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2ant
RMSD bond length	0.008
RMSD bond angle	1.020
Data reduction software	MOSFLM
Data scaling software	CCP4
Phasing software	AMoRE
Refinement software	TNT (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	3.120
High resolution limit [Å]	2.900	2.940
Rmerge	0.046	0.130
Number of reflections	23603
<I/σ(I)>	13.6	5.6
Completeness [%]	95.4	87.8
Redundancy	2.5	2.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Batch method *	6.9		30.6% W/V PEG4000, 35% V/V GLYCEROL, 30 MM CACODYLATE, PH 6.9

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	protein	10 (mg/ml)
2	1	1	PEG4000	30.6 (%(w/v))
3	1	1	glycerol	35 (%(v/v))
4	1	1	cacodylate	30 (mM)