4FON

High Energy Remote SAD structure solution of Proteinase K from the 37.8 keV Tellurium K edge

Experimental procedure

Experimental method	LAUE
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID15C
Synchrotron site	ESRF
Beamline	ID15C
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2011-11-21
Detector	MARRESEARCH
Wavelength(s)	0.328
Spacegroup name	P 43 21 2
Unit cell lengths	68.180, 68.180, 102.688
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	11.890 - 1.050
R-factor	0.11286
Rwork	0.112
R-free	0.13073
Structure solution method	SAD
RMSD bond length	0.008
RMSD bond angle	1.342
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	SHELXS
Refinement software	REFMAC (5.6.0117)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	12.000	1.070
High resolution limit [Å]	1.050	1.050
Rmerge	0.099	0.660
Number of reflections	111263
<I/σ(I)>	13.4	2.1
Completeness [%]	98.4	99.6
Redundancy	7.7	7.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	295	1 uL 60 mg/mL protein + 1 uL reservoir (1 mL saturated potassium tellurate), cryo-solution: 70% crystallization solution, 30% ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 295K
1	VAPOR DIFFUSION, HANGING DROP	7	295	1 uL 60 mg/mL protein + 1 uL reservoir (1 mL saturated potassium tellurate), cryo-solution: 70% crystallization solution, 30% ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 295K