1F13

RECOMBINANT HUMAN CELLULAR COAGULATION FACTOR XIII

Experimental procedure

Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1996-09-05
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	134.590, 72.780, 101.050
Unit cell angles	90.00, 106.08, 90.00

Refinement procedure

Resolution	40.000 - 2.100
R-factor	0.183
Rwork	0.183
R-free	0.23600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ggt
RMSD bond length	0.010
RMSD bond angle	1.562
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.1)
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	99.000	2.180
High resolution limit [Å]	2.100	2.100
Rmerge	0.103	0.300
Total number of observations	293385 *
Number of reflections	89672
<I/σ(I)>	10.7	2.2
Completeness [%]	81.6	40.2
Redundancy	3.3	1.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	6.2		THE PROTEIN WAS CRYSTALLIZED FROM 1-2% PEG 6000, 100 MM MES, PH 6.2-6.4

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	2-4 (mg/ml)
2	1	reservoir	MES	100 (mM)
3	1	reservoir	PEG6000	1-2 (%(w/v))