Crystal Structure of the CTP1L Endolysin Reveals How Its Activity Is Regulated by a Secondary Translation Product.

Dunne M, Leicht S, Krichel B, Mertens HD, Thompson A, Krijgsveld J, Svergun DI, Gómez-Torres N, Garde S, Uetrecht C, Narbad A, Mayer MJ, Meijers R
J Biol Chem 291(10):4882-93 (2016 Mar 4)
PMID: 26683375
doi: 10.1074/jbc.M115.671172 		Submitted to SASBDB: 2015 Jan 19
Published in SASBDB:

SASDAD7 – Structure of a complex between full length and truncated CTP1L endolysin

Endolysin experimental SAS data
CRYSOL model
Sample: Endolysin , 33 kDa Clostridium phage phiCTP1 protein
Buffer: 20 mM HEPES, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 17
RgGuinier 3.7 nm
Dmax 13.8 nm
VolumePorod 95 nm3

SASDAE7 – Structure of a complex between full length and truncated CS74L endolysin

Endolysin CS74L experimental SAS data
DAMMIF model
Sample: Endolysin CS74L , 31 kDa Clostridium phage phi8074-B1 protein
Buffer: 20 mM HEPES, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 17
RgGuinier 3.6 nm
Dmax 14.0 nm
VolumePorod 79 nm3