9QRP

Thermus thermophilus seryl-tRNA synthetase bound to tRNA(ser)(GGA) and seryl-adenylate analogue.

This is a non-PDB format compatible entry.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	LURE BEAMLINE DW32
Synchrotron site	LURE
Beamline	DW32
Temperature [K]	138
Detector technology	IMAGE PLATE
Collection date	1994-11-19
Detector	MAR scanner 300 mm plate
Wavelength(s)	0.9
Spacegroup name	P 21 21 21
Unit cell lengths	121.040, 125.810, 117.620
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.990 - 2.700
R-factor	0.1866
Rwork	0.184
R-free	0.22960
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.002
RMSD bond angle	0.530
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	PHENIX (1.21.2_5419)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.820
High resolution limit [Å]	2.700	2.700
Rmerge	0.069	0.225
Number of reflections	45116	2759
<I/σ(I)>	10.5
Completeness [%]	90.7	48.6
Redundancy	3.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.2	293	10 microliter hanging drops containing 25 mM Tris-maleate/NaOH buffer at pH 7.2,2.5 mM MgC12,20% saturated (V/V) ammonium sulphate, 1 mM NaN3, 2.6 mg/ml tRNA(ser) and 5.6 mg/ml seryl-tRNA synthetase (stoichiometric ratio of 1.5 tRNA molecules to one enzyme dimer), were equil- ibrated at room temperature against 32% saturated ammonium sulphate.