1KQL

Crystal structure of the C-terminal region of striated muscle alpha-tropomyosin at 2.7 angstrom resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CHESS BEAMLINE A1
Synchrotron site	CHESS
Beamline	A1
Temperature [K]	95
Detector technology	CCD
Collection date	2001-04-20
Detector	ADSC QUANTUM 4
Wavelength(s)	0.909
Spacegroup name	P 64 2 2
Unit cell lengths	137.202, 137.202, 40.071
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	9999.000 * - 2.700
R-factor	0.251 *
Rwork	0.252
R-free	0.28900 *
Structure solution method	Molecular replacement using a specially built model
Starting model (for MR)	a specially built 56-residue two-stranded coiled-coil that contains a 24 residue fragment from the high resolution structure of the GCN4 leucine zipper
RMSD bond length	0.007
RMSD bond angle	1.012 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	9999.000 *	2.690
High resolution limit [Å]	2.600	2.600
Rmerge	0.052	0.217
Total number of observations	86920 *
Number of reflections	7221
<I/σ(I)>	34.9	9.14
Completeness [%]	99.9	99.9
Redundancy	12	8.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	7.5 *	22 *	PEG 550 monomethylether, glycerol, sodium chloride, magnesium acetate, bicine, tris buffer, dithiothreitol, pH 8.3, VAPOR DIFFUSION, SITTING DROP, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5 (mg/ml)
10	1	reservoir		100 (mM)
11	1	reservoir		20 (mM)
12	1	reservoir	bicine	200 (mM)	pH8.3
2	1	drop	glycerol	20 (%)
3	1	drop	dithiothreitol	1 (mM)
4	1	drop	Tris	10 (mM)	pH7.5
5	1	drop	PEG550MME	12 (%)
6	1	drop	Bicine	60 (mM)	pH9.0
7	1	drop		300 (mM)
8	1	drop		60 (mM)
9	1	reservoir	PEG550 MME	4 (%)