1OK0

Crystal Structure of Tendamistat

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X11
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X11
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-02-15
Detector	MAR scanner 345 mm plate
Spacegroup name	P 21 21 21
Unit cell lengths	25.680, 40.780, 60.950
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	10.000 - 0.930
R-factor	0.1026
R-free	0.13000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1hoe
RMSD bond length	0.015
RMSD bond angle	0.033
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	SHELXL-97

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.000	0.950
High resolution limit [Å]	0.930	0.930
Rmerge	0.054	0.326
Total number of observations	261064 *
Number of reflections	41072 *	2167 *
<I/σ(I)>	20.3	4.3
Completeness [%]	93.5	79.9
Redundancy	6.9	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	1.3 *		20MG OF LYOPHILIZED PROTEIN WERE DISSOLVED IN 1ML OF DOUBLE-DISTILLED WATER. USING THE HANGING DROP METHOD WITH DROPS OF 2MUL PROTEIN SOLUTION (20 MG/ML) AND 2MUL RESERVOIR SOLUTION (0.1-0.5 M NACL ADJUSTED TO PH 1.3 WITH HYDROCHLORIC ACID), YIELDED TUFT-SHAPED AGGLOMERATES OF ESSENTIALLY ONE-DIMENSIONAL CRYSTALS. STREAK SEEDING {EM VIA} A CAT WHISKER AFTER TOUCHING THESE AGGLOMERATES GAVE SINGLE CRYSTALS WITH DIMENSIONS UP TO 0.1 X 0.01 X 0.01MM^3

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	reservoir		0.1-0.5 (M)	pH1.3