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Hydrolase PDB-id
2bxz
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Protein chain
580 a.a. *
Ligands
TRS
TRE ×2
GLC ×2
BME
Metal ions
_MG
Waters ×856

* Residue conservation analysis
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PDB id: 2bxz
Name: Hydrolase
Title: Is radiation damage dependent on the dose-rate used during macromolecular crystallography data collection

Structure:
Maltooligosyltrehalose trehalohydrolase. Chain: a. Engineered: yes

Source:
Deinococcus radiodurans. Organism_taxid: 243230. Strain: r1. Expressed in: escherichia coli. Expression_system_taxid: 469008.

UniProt:
Q9RX51 (Q9RX51_DEIRA) Pfam  
Seq:
Struc:
Seq:
Struc:
Seq: 600 a.a.
Struc: 580 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Resolution:
1.75Å

R-factor:
0.150

R-free:
0.188

Authors:
H.-K.S.Leiros,J.Timmins,R.B.G.Ravelli,S.M.Mcsweeney

Key ref:
H.K.Leiros et al. (2006). Is radiation damage dependent on the dose rate used during macromolecular crystallography data collection?. Acta Crystallogr D Biol Crystallogr, 62, 125-132. [PubMed id: 16421442] [DOI: 10.1107/S0907444905033627]

Date:
28-Jul-05

Release date:
06-Feb-06

Related entries:
2bhu crystal structure of deinococcus radiodurans maltooligosyltrehalose trehalohydrolase
2bhy crystal structure of deinococcus radiodurans maltooligosyltrehalose trehalohydrolase in complex with trehalose
2bhz crystal structure of deinococcus radiodurans maltooligosyltrehalose trehalohydrolase in complex with maltose
2bxy is radiation damage dependent on the dose- rate used during macromolecular crystallography data collection
2by0 is radiation damage dependent on the dose- rate used during macromolecular crystallography data collection
2by1 is radiation damage dependent on the dose- rate used during macromolecular crystallography data collection
2by2 is radiation damage dependent on the dose- rate used during macromolecular crystallography data collection
2by3 is radiation damage dependent on the dose- rate used during macromolecular crystallography data collection
2by5 is radiation damage dependent on the dose- rate used during macromolecular crystallography data collection
2by6 is radiation damage dependent on the dose- rate used during macromolecular crystallography data collection
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    Key reference    
 
 
DOI no: 10.1107/S0907444905033627 Acta Crystallogr D Biol Crystallogr 62:125-132 (2006)
PubMed id: 16421442  
 
 
Is radiation damage dependent on the dose rate used during macromolecular crystallography data collection?
H.K.Leiros, J.Timmins, R.B.Ravelli, S.M.McSweeney.
 
  ABSTRACT  
 
This paper focuses on the radiation-damage effects when applying the same total X-ray dose to protein crystals at different dose rates. These experiments have been performed on both a selenomethionated protein and on bovine trypsin using dose rates that span nearly two orders of magnitude. The results show no clear dose-rate effect on the global indicators of radiation damage, but a small measurable dose-rate effect could be found when studying specific radiation damage. It is hypothesized that this observed dose-rate effect relates to differences in the steady-state free-radical concentration.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 (a) Illustrations of the disulfide bond from Cys395 to the Bme residue and (b) the seven SeMet residues (Mse), with the corresponding vector difference map from the drMTH-Rate75 burn displayed at +4 [sigma] (red) and -4 [sigma] (green).
Figure 5.
Figure 5 Active site of BT: an illustration of the binding pocket in BT with the vector difference map from BT-Rate24 contoured at +4 [sigma] (red) and -4 [sigma] (green). The inhibitor benzamidine (Bza), Asp189, Ser190, Tyr228 and some surrounding water molecules are shown.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 125-132) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18701720 J.P.Colletier, D.Bourgeois, B.Sanson, D.Fournier, J.L.Sussman, I.Silman, and M.Weik (2008).
Shoot-and-Trap: use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography.
  Proc Natl Acad Sci U S A, 105, 11742-11747.
PDB codes: 2vja 2vjb 2vjc 2vjd 2vt6 2vt7
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.