 |
PDBsum entry 6s1d
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Plant protein
|
PDB id
|
|
|
|
6s1d
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Plant protein
|
|
|
Title:
|
|
Structure of thaumatin determined at swissfel using native-sad at 4.57 kev from 20,000 diffraction patterns
|
|
Structure:
|
|
Thaumatin-1. Chain: a. Synonym: thaumatin i. Engineered: yes
|
|
Source:
|
|
Thaumatococcus daniellii. Katemfe. Organism_taxid: 4621. Expressed in: thaumatococcus daniellii. Expression_system_taxid: 4621
|
|
Resolution:
|
|
|
2.65Å
|
R-factor:
|
0.155
|
R-free:
|
0.196
|
|
|
Authors:
|
|
K.Nass,R.Cheng,L.Vera,A.Mozzanica,S.Redford,D.Ozerov,S.Basu,D.James, G.Knopp,C.Cirelli,I.Martiel,C.Casadei,T.Weinert,P.Nogly, P.Skopintsev,I.Usov,F.Leonarski,T.Geng,M.Rappas,A.S.Dore,R.Cooke, S.Nasrollahi Shirazi,F.Dworkowski,M.Sharpe,N.Olieric,M.O.Steinmetz, G.Schertler,R.Abela,L.Patthey,B.Schmitt,M.Hennig,J.Standfuss,M.Wang, J.C.Milne
|
|
Key ref:
|
|
K.Nass
et al.
(2020).
Advances in long-wavelength native phasing at X-ray free-electron lasers.
IUCrJ,
7,
965-975.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
18-Jun-19
|
Release date:
|
15-Jul-20
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P02883
(THM1_THADA) -
Thaumatin I from Thaumatococcus daniellii
|
|
|
|
Seq:
Struc:
|
|
|
|
235 a.a.
207 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
|
*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
IUCrJ
7:965-975
(2020)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Advances in long-wavelength native phasing at X-ray free-electron lasers.
|
|
K.Nass,
R.Cheng,
L.Vera,
A.Mozzanica,
S.Redford,
D.Ozerov,
S.Basu,
D.James,
G.Knopp,
C.Cirelli,
I.Martiel,
C.Casadei,
T.Weinert,
P.Nogly,
P.Skopintsev,
I.Usov,
F.Leonarski,
T.Geng,
M.Rappas,
A.S.Doré,
R.Cooke,
S.Nasrollahi Shirazi,
F.Dworkowski,
M.Sharpe,
N.Olieric,
C.Bacellar,
R.Bohinc,
M.O.Steinmetz,
G.Schertler,
R.Abela,
L.Patthey,
B.Schmitt,
M.Hennig,
J.Standfuss,
M.Wang,
C.J.Milne.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Long-wavelength pulses from the Swiss X-ray free-electron laser (XFEL) have been
used for de novo protein structure determination by native
single-wavelength anomalous diffraction (native-SAD) phasing of serial
femtosecond crystallography (SFX) data. In this work, sensitive anomalous
data-quality indicators and model proteins were used to quantify improvements in
native-SAD at XFELs such as utilization of longer wavelengths, careful
experimental geometry optimization, and better post-refinement and partiality
correction. Compared with studies using shorter wavelengths at other XFELs and
older software versions, up to one order of magnitude reduction in the required
number of indexed images for native-SAD was achieved, hence lowering sample
consumption and beam-time requirements significantly. Improved data quality and
higher anomalous signal facilitate so-far underutilized de novo structure
determination of challenging proteins at XFELs. Improvements presented in this
work can be used in other types of SFX experiments that require accurate
measurements of weak signals, for example time-resolved studies.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
