Journal: J.Mol.Biol. / Year: 2006 Title: Direct Evidence for a Glutamate Switch Necessary for Substrate Recognition: Crystal Structures of Lysine Epsilon-Aminotransferase (Rv3290C) from Mycobacterium Tuberculosis H37Rv. Authors: Tripathi, S.M. / Ramachandran, R.
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1.5418 Å / Relative weight: 1
Reflection
Resolution: 2→28.49 Å / Num. obs: 39961 / % possible obs: 97.7 % / Observed criterion σ(I): 20 / Redundancy: 5 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 13.7
Reflection shell
Resolution: 2→2.11 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.55 / Mean I/σ(I) obs: 2.8 / % possible all: 99.6
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Processing
Software
Name
Version
Classification
REFMAC
5.2.0005
refinement
MOSFLM
datareduction
SCALA
datascaling
AMoRE
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→89.44 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.958 / SU B: 2.783 / SU ML: 0.076 / Cross valid method: THROUGHOUT / ESU R: 0.121 / ESU R Free: 0.112 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUE 1-14 ARE DISORDERED. SUBSTRATE L- LYSINE IS COVALENTLY LINKED WITH PLP
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.176
2015
5 %
RANDOM
Rwork
0.149
-
-
-
obs
0.15
37946
97.1 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK