Structure of the 4-hydroxy-tetrahydrodipicolinate synthase from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV and the phylogeny of the aminotransferase pathway

Schmitz, R.A.; Dietl, A.; Müller, M.; Berben, T.; Op den Camp, H.J.M.; Barends, T.R.M.

doi:10.1107/S2053230X20005294

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 2
A Tris–glycine 4–20% gradient gel (Coomassie staining) of the protein preparation (lane H). Bands H1–H7 were excised for peptide mass fingerprinting. Band H4 was identified as M. fumariolicum SolV DapA (MfumV2_0415), bands H1 and H3 as the large and small subunits of the [NiFe] hydrogenase, respectively (MfumV2_0979 and MfumV2_0978), and band H2 as a degradation product of the large subunit. Band H5 was identified as elongation factor Ts (MfumV2_2094) and band H7 as the ClpB chaperone (MfumV2_0146). No match was found for band H6. Lane MW contains a molecular-weight ladder, with the molecular masses indicated in kDa on the left.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 76| Part 5| May 2020| Pages 199-208

https://doi.org/10.1107/S2053230X20005294

Open

access

Follow Acta Cryst. F

Search IUCr Journals		doi		Advanced search
Author		volume	page