1GME

Crystal structure and assembly of an eukaryotic small heat shock protein

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-3
Synchrotron site	ESRF
Beamline	ID14-3
Temperature [K]	120
Detector technology	CCD
Collection date	1999-09-15
Detector	MARRESEARCH
Spacegroup name	H 3 2
Unit cell lengths	171.645, 171.645, 124.157
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 - 2.700
R-factor	0.231
Rwork	0.231
R-free	0.28600
Structure solution method	MAD
RMSD bond length	0.008 *
RMSD bond angle	1.400 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	SnB (V. 2.1)
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.790
High resolution limit [Å]	2.700 *	2.650
Rmerge	0.040	0.164
Total number of observations	170065 *
Number of reflections	19276
<I/σ(I)>	13	4
Completeness [%]	94.6	96.7
Redundancy	5.9	5.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	other *	7 *	20 *	PROTEIN WAS CRYSTALLIZED FROM 26-29% PEG400, 0.2M SODIUM CITRATE, 0.1M TRIS/HCL PH8.5, pH 8.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG400	26-29 (%(v/v))
2	1	reservoir	sodium citrate	0.2 (M)
3	1	reservoir	Tris-HCl	0.1 (M)	pH8.5
4	1	drop	EDTA	1 (mM)
5	1	drop	dithiothreitol	2 (mM)
6	1	drop	Tris-HCl	10 (mM)	pH7.0
7	1	drop	protein	8 (mg/ml)