1MNF

Domain motions in GroEL upon binding of an oligopeptide

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Spacegroup name	P 1 21 1
Unit cell lengths	135.415, 260.694, 148.691
Unit cell angles	90.00, 100.94, 90.00

Refinement procedure

Resolution	20.000 * - 3.000
R-factor	0.236
Rwork	0.236
R-free	0.25900
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	20.700 *
Data reduction software	HKL-2000
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	CNS

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000 *
High resolution limit [Å]	3.000 *	3.000 *
Rmerge	0.099 *	0.147 *
Total number of observations	436111 *
Number of reflections	167654 *
Completeness [%]	84.4 *	73.9 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7	28 *	Boisvert, D.C., (1996) Nat.Struct.Biol., 3, 170. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	25 (mg/ml)
10	1	reservoir	sodium azide	0.01 (%)
2	1	reservoir	PEG8000	2.2 (%(w/v))
3	1	reservoir	Bis-Tris-propane	25 (mM)	pH7.0
4	1	reservoir	ethylene glycol	15 (%)
5	1	reservoir	glycerol	5 (%)
6	1	reservoir		2.5 (mM)
7	1	reservoir		50 (mM)
8	1	reservoir		9 (mM)