1LOK

The 1.20 Angstrom Resolution Crystal Structure of the Aminopeptidase from Aeromonas proteolytica Complexed with Tris: A Tale of Buffer Inhibition

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-BM-C
Synchrotron site	APS
Beamline	14-BM-C
Temperature [K]	100
Detector technology	CCD
Collection date	2000-02-11
Detector	ADSC QUANTUM 4
Wavelength(s)	1.0000
Spacegroup name	P 61 2 2
Unit cell lengths	108.338, 108.338, 93.519
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.000 * - 1.200
R-factor	0.145
Rwork	0.158
R-free	0.17600 *
Structure solution method	FOURIER SYNTHESIS
Starting model (for MR)	1amp
RMSD bond length	0.018
RMSD bond angle	0.032
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000 *	1.250
High resolution limit [Å]	1.200 *	1.200 *
Rmerge	0.057 *	0.290 *
Total number of observations	1348266 *
Number of reflections	117248 *
Completeness [%]	99.0 *	98
Redundancy	15

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion *	8	295	Tris, potassium thiocyanate, sodium chloride, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	16 (mg/ml)
2	1	drop	Tris	10 (mM)	pH8.0
3	1	drop	KSCN	10 (mM)
4	1	drop		0.4 (M)
5	1	reservoir	Tris	100 (mM)	pH8.0
6	1	reservoir	KSCN	100 (mM)
7	1	reservoir		4.5 (M)