1KV3

HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-BM-D
Synchrotron site	APS
Beamline	14-BM-D
Temperature [K]	100
Detector technology	CCD
Collection date	2000-11-29
Detector	ADSC QUANTUM 4
Wavelength(s)	1.0
Spacegroup name	P 21 21 21
Unit cell lengths	132.479, 168.797, 238.568
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	51.790 - 2.800
R-factor	0.233
Rwork	0.233
R-free	0.27200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	factor XIIIa PDB entry 1GGU
RMSD bond length	0.013
RMSD bond angle	26.300 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	51.800 *	2.980
High resolution limit [Å]	2.800	2.800
Rmerge	0.085	0.470
Total number of observations	1141553 *
Number of reflections	124870
Completeness [%]	94.6	88.8
Redundancy	4.4	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7 *	277	50 mM MES, pH 6.6, 200 mM NaCl, 50 mM MgCl2, 6-8% PEG3350 and 5 mM DTT, VAPOR DIFFUSION, HANGING DROP, temperature 4K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
10	1	reservoir	dithiothreitol	5 (mM)
2	1	drop	HEPES	20 (mM)	pH7.0
3	1	drop	EDTA/EGTA	1 (mM)
4	1	drop	dithiothreitol	5 (mM)
5	1	drop	glycerol	20 (%(v/v))
6	1	reservoir	MES	50 (mM)	pH6.6
7	1	reservoir		200 (mM)
8	1	reservoir		50 (mM)
9	1	reservoir	PEG3350	6-8 (%)