1KV0

Cis/trans Isomerization of Non-prolyl Peptide Bond Observed in Crystal Structure of an Scorpion Toxin

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	PHOTON FACTORY BEAMLINE BL-18B
Synchrotron site	Photon Factory
Beamline	BL-18B
Temperature [K]	293
Detector technology	CCD
Collection date	2000-12-24
Detector	ADSC QUANTUM 4
Wavelength(s)	1.0
Spacegroup name	P 31 2 1
Unit cell lengths	32.758, 32.758, 176.822
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	29.300 * - 1.400
R-factor	0.14416
Rwork	0.142
R-free	0.16400 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1sn1
RMSD bond length	0.017 *
RMSD bond angle	1.983 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	AMoRE
Refinement software	REFMAC (5.1.04)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	29.300	1.480
High resolution limit [Å]	1.400	1.400
Rmerge	0.040	0.201
Total number of observations	57131 *
Number of reflections	19260
<I/σ(I)>		3.6
Completeness [%]	85.8	74.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8.5	293	ammonium sulfate, Tris-HCl, Ethanol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	ammonium sulfate	0.65 (M)
3	1	reservoir	Tris-HCl	100 (mM)	pH8.5
4	1	reservoir	ethanol	1 (%(v/v))