1ORF

The Oligomeric Structure of Human Granzyme A Reveals the Molecular Determinants of Substrate Specificity

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.3
Synchrotron site	ALS
Beamline	5.0.3
Temperature [K]	100
Detector technology	CCD
Collection date	2002-06-02
Detector	ADSC QUANTUM 4
Wavelength(s)	1
Spacegroup name	C 2 2 21
Unit cell lengths	115.034, 145.022, 39.555
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.400
R-factor	0.19137
Rwork	0.191
R-free	0.23200 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dst
RMSD bond length	0.013
RMSD bond angle	1.544 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	EPMR
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.490
High resolution limit [Å]	2.400	2.400
Rmerge	0.103 *	0.417 *
Total number of observations	175040 *
Number of reflections	13373 *
Completeness [%]	99.0 *	94 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6 *	17 *	Tris pH 8.5, PEG 4000, lithium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	MES	50 (mM)	pH6.0
2	1	drop		50 (mM)
3	1	drop	protein	10 (mg/ml)
4	1	drop	D-Phe-Pro-Arg-CMK	2.9 (mM)
5	1	reservoir	Tris	0.1 (M)	pH8.5
6	1	reservoir		0.2 (mM)
7	1	reservoir	PEG4000	13-18 (%(v/v))