1VIX

Crystal structure of a putative peptidase T

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 32-ID
Synchrotron site	APS
Beamline	32-ID
Detector technology	CCD
Detector	MARRESEARCH
Wavelength(s)	0.9794
Spacegroup name	P 21 21 21
Unit cell lengths	115.270, 145.787, 77.121
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	32.690 - 2.500
Rwork	0.256
R-free	0.30300
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.000 *
Data reduction software	MOSFLM
Data scaling software	SCALA
Refinement software	REFMAC (4.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	32.690	2.640
High resolution limit [Å]	2.500	2.500
Rmerge	0.068	0.614
Number of reflections	34894
<I/σ(I)>	12.2	1.8
Completeness [%]	77.0	62.7
Redundancy	4.1	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5 *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	HEPES	10 (mM)	pH7.5
2	1	drop		150 (mM)
3	1	drop	methionine	10 (mM)
4	1	drop	glycerol	10 (%)
5	1	drop	dithiothreitol	5 (mM)
6	1	drop	protein	10 (mg/ml)