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PDBsum entry 5mg0
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PDB id:
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Transferase
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Title:
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Structure of pas-gaf fragment of deinococcus phytochrome by serial femtosecond crystallography
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Structure:
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Bacteriophytochrome. Chain: a. Synonym: phytochrome-like protein. Engineered: yes. Mutation: yes
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Source:
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Deinococcus radiodurans (strain atcc 13939 / dsm 20539 / jcm 16871 / lmg 4051 / nbrc 15346 / ncimb 9279 / r1 / vkm b-1422). Organism_taxid: 243230. Strain: atcc 13939 / dsm 20539 / jcm 16871 / lmg 4051 / nbrc 15346 / ncimb 9279 / r1 / vkm b-1422. Gene: bphp, dr_a0050. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008
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Resolution:
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1.65Å
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R-factor:
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0.174
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R-free:
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0.203
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Authors:
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E.S.Burgie,F.D.Fuller,S.Gul,M.D.Miller,I.D.Young,A.S.Brewster, J.Clinger,P.Aller,P.Braeuer,C.Hutchison,R.Alonso-Mori,J.Kern, V.K.Yachandra,J.Yano,N.K.Sauter,G.N.Phillips Jr.,R.D.Vierstra, A.M.Orville
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Key ref:
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F.D.Fuller
et al.
(2017).
Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers.
Nat Methods,
14,
443-449.
PubMed id:
DOI:
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Date:
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20-Nov-16
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Release date:
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22-Feb-17
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PROCHECK
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Headers
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References
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Q9RZA4
(BPHY_DEIRA) -
Bacteriophytochrome from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
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Seq:
Struc:
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755 a.a.
322 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 7 residue positions (black
crosses)
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Enzyme class:
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E.C.2.7.13.3
- histidine kinase.
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Reaction:
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ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
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ATP
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+
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protein L-histidine
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=
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ADP
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+
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protein N-phospho-L-histidine
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Nat Methods
14:443-449
(2017)
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PubMed id:
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Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers.
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F.D.Fuller,
S.Gul,
R.Chatterjee,
E.S.Burgie,
I.D.Young,
H.Lebrette,
V.Srinivas,
A.S.Brewster,
T.Michels-Clark,
J.A.Clinger,
B.Andi,
M.Ibrahim,
E.Pastor,
C.de Lichtenberg,
R.Hussein,
C.J.Pollock,
M.Zhang,
C.A.Stan,
T.Kroll,
T.Fransson,
C.Weninger,
M.Kubin,
P.Aller,
L.Lassalle,
P.Bräuer,
M.D.Miller,
M.Amin,
S.Koroidov,
C.G.Roessler,
M.Allaire,
R.G.Sierra,
P.T.Docker,
J.M.Glownia,
S.Nelson,
J.E.Koglin,
D.Zhu,
M.Chollet,
S.Song,
H.Lemke,
M.Liang,
D.Sokaras,
R.Alonso-Mori,
A.Zouni,
J.Messinger,
U.Bergmann,
A.K.Boal,
J.M.Bollinger,
C.Krebs,
M.Högbom,
G.N.Phillips,
R.D.Vierstra,
N.K.Sauter,
A.M.Orville,
J.Kern,
V.K.Yachandra,
J.Yano.
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ABSTRACT
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X-ray crystallography at X-ray free-electron laser sources is a powerful method
for studying macromolecules at biologically relevant temperatures. Moreover,
when combined with complementary techniques like X-ray emission spectroscopy,
both global structures and chemical properties of metalloenzymes can be obtained
concurrently, providing insights into the interplay between the protein
structure and dynamics and the chemistry at an active site. The implementation
of such a multimodal approach can be compromised by conflicting requirements to
optimize each individual method. In particular, the method used for sample
delivery greatly affects the data quality. We present here a robust way of
delivering controlled sample amounts on demand using acoustic droplet ejection
coupled with a conveyor belt drive that is optimized for crystallography and
spectroscopy measurements of photochemical and chemical reactions over a wide
range of time scales. Studies with photosystem II, the phytochrome
photoreceptor, and ribonucleotide reductase R2 illustrate the power and
versatility of this method.
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