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   1 e been phased using external information via molecular replacement.                                  
     2 phate), is determined to 2.3 A resolution by molecular replacement.                                  
     3 ructure of H256A to a resolution of 2.4 A by molecular replacement.                                  
     4 hine has been solved at 1.85-A resolution by molecular replacement.                                  
     5         An x-ray structure was determined by molecular replacement.                                  
     6 roup P41212, and the structure was solved by molecular replacement.                                  
     7 he corresponding X-ray crystal structures by molecular replacement.                                  
     8 e has been determined to 2.5 A resolution by molecular replacement.                                  
     9 tfC crystal structure was solved at 2.7 A by molecular replacement.                                  
    10 ylated human IFN-beta at 2.2-A resolution by molecular replacement.                                  
    11  resolution, and the structure was solved by molecular replacement.                                  
    12  the RCs in the unit cell were determined by molecular replacement.                                  
    13 Triton X-100 and the structure was solved by molecular replacement.                                  
    14  structure was solved to 1.5-A resolution by molecular replacement.                                  
    15  enzyme in phenazine biosynthesis, solved by molecular replacement.                                  
    16 ) was also determined at 2.6 A resolution by molecular replacement.                                  
    17 lized at pH 6.25 and its structure solved by molecular replacement.                                  
    18 iously, it was possible to use the method of molecular replacement.                                  
    19  been determined to a resolution of 3.0 A by molecular replacement.                                  
    20 on-inhibited W197I variant was determined by molecular replacement (2.2 A); it revealed a stabilized 
  
  
    23 xMDFF, either fails to produce a solution by molecular replacement alone or produces an inaccurate st
  
    25 pection of the X-ray diffraction pattern and molecular replacement analysis revealed the orientation 
    26 ex was solved at a resolution of 3.0 A using molecular replacement and constitutes the first reported
    27 ex was solved at a resolution of 2.5 A using molecular replacement and constitutes the first reported
    28 d to 2.1 A resolution using a combination of molecular replacement and isomorphous replacement and re
  
    30 ylate has been solved using a combination of molecular replacement and noncrystallographic symmetry a
  
  
  
  
  
    36 from Arabidopsis thaliana has been solved by molecular replacement and refined at the resolution of 1
    37 noclonal antibody (Mab231) was determined by molecular replacement and refined in a triclinic cell to
  
    39 =59.15 A, c=94.44 A) have been determined by molecular replacement and refined versus data to 2.0 A a
    40 .9 A resolution; the structure was solved by molecular replacement and refined with an R-factor of 0.
    41 Man-alpha 1,3-Man-OMe complex, determined by molecular replacement and refined with X-PLOR using NCS 
  
  
  
    45  placed in the crystallographic unit cell by molecular replacement, and how initial phases computed f
  
    47 The SM3-MUC1 peptide structure was solved by molecular replacement, and the current model is refined 
    48 6 (lambda(em)max = 486 nm) was determined by molecular replacement, and the model was refined at 1.65
    49     These crystalline properties permitted a molecular replacement approach based upon a beta-hairpin
  
    51     In this review, we discuss a single-cell molecular replacement approach which should arguably adv
  
  
    54 esidues Asp 2-Asn 762 has been determined by molecular replacement at 1.9 A resolution and refined to
  
    56 d the crystal structures of AgaA and AgaB by molecular replacement at 3.2- and 1.8 A-resolution, resp
    57 s cerevisiae chorismate mutase was solved by molecular replacement at a resolution of 2.8 angstroms u
    58 ture determined to 4.4-A resolution by using molecular replacement based on the structure of the beef
  
  
    61 inal Src kinase (CSK) has been determined by molecular replacement, co-complexed with the protein kin
  
    63 ended in steps to 3.0 angstrom resolution by molecular replacement electron density modification and 
  
  
  
  
    68 m for structure determination of lysozyme by molecular replacement followed by crystallographic refin
    69 itor, were determined at 2.0 A resolution by molecular replacement from a second crystal form and wer
    70 native crystals in the space group P3(1), by molecular replacement from the 2.8 A model (1F88) solved
  
  
    73 tate at 2.03 A resolution that was solved by molecular replacement in the space group P6(5) with two 
  
    75 tructures are determined using the method of molecular replacement, in which known related structures
    76 l in phasing crystallographic data for which molecular replacement is hindered by the absence of suff
    77 nderstanding of the signal-to-noise ratio in molecular replacement leads to the finding that, with da
  
    79  crystal structure of hCBG was solved by the molecular replacement method and refined at 2.7 A resolu
  
  
  
    83 of IVD was solved at 2.6 A resolution by the molecular replacement method and was refined to an R-fac
  
    85 on method for the first crystal form and the molecular replacement method for the second crystal form
  
    87 initial solution was determined by using the molecular replacement method using the structure of the 
    88 otein or peptide can be determined using the molecular replacement method with the help of the GST st
  
  
  
  
  
  
    95 id) complex were determined with the help of molecular replacement methods to 2.0A and 2.3A resolutio
    96 bound to domain VI of calpain, determined by molecular replacement methods to 2.5A and 2.2A resolutio
    97 tic domain joined by a linker, was solved by molecular replacement methods using independent search m
    98 human plasminogen (K5HPg) has been solved by molecular replacement methods using K1HPg as a model and
    99 ccus surface protein, has been determined by molecular replacement methods using K4Pg as a model, and
  
  
  
  
   104 n from electron cryomicroscopy was used as a molecular replacement model for initial phase determinat
  
  
   107 re we show that, contrary to current belief, molecular replacement need not be restricted to the use 
  
  
   110 pid carrier proteins, may also contribute to molecular replacement of disc membrane DHA-phospholipids
  
  
   113  D has been solved to 2.3-A resolution using molecular replacement phases derived from human oxyhemog
   114 CD has been solved to 3.0 A resolution using molecular replacement phases derived from the structure 
  
  
   117 he signal-to-noise ratio in likelihood-based molecular replacement searches has been developed to acc
   118 A tungstate derivative confirmed the initial molecular replacement solution and identified an anion b
   119 tant has been solved at 1.62 A resolution by molecular replacement starting from the structure of the
  
   121 sential for synaptic potentiation by using a molecular replacement strategy designed to dissociate Ra
  
   123 pal pyramidal neurons, we used a single-cell molecular replacement strategy to replace all endogenous
  
   125 ral role in X-ray structure determination by molecular replacement, such information is rarely used i
   126  The crystal structure has been solved using molecular replacement techniques and refined by simulate
  
  
   129     The resulting model was used to solve by molecular replacement the X-ray structure of l-sfAFP to 
  
   131 ycogenin and UDP-glucose/Mn2+ were solved by molecular replacement to 1.9 A using the orthorhombic cr
  
  
  
   135 ontaining tripeptide have been determined by molecular replacement to 3.5 A and 2.4 A resolutions, re
  
  
  
   139 berculosis antigen 85B (ag85B), initially by molecular replacement using antigen 85C as a probe.     
   140  activity, was solved at 1.5 A resolution by molecular replacement using as the search model the solu
   141 OPS) from Escherichia coli was determined by molecular replacement using coordinates given to us by R
   142  A. aeolicus enzyme, which was determined by molecular replacement using E. coli KDO8PS as a model.  
  
   144 ine was determined to 2.18 A resolution with molecular replacement using rat PITPalpha (77% sequence 
  
   146      The structural solution was obtained by molecular replacement using superimposed polyalanine coo
   147  structure determined to 2.0 A resolution by molecular replacement using the coordinates of a truncat
  
  
  
   151 re obtained, and the structure was solved by molecular replacement using the CsdB coordinates combine
   152 at 1.85 A (cubic), respectively, resolved by molecular replacement using the homologous avian infecti
   153 m) was determined to a resolution of 2.7A by molecular replacement using the human apo-N-lobe and the
   154 murium have been determined by the method of molecular replacement using the known structure of the h
   155  the presence of 0.1 M Mg(2+), was solved by molecular replacement using the model of cowpea chloroti
   156 se from Bacillus subtilis, was determined by molecular replacement using the muconate lactonizing enz
   157 eductase superfamily, has been determined by molecular replacement using the NADPH-bound form of the 
   158 f the PLP-bound holoenzyme was determined by molecular replacement using the Pseudomonas fluorescens 
   159 l structure of human sfALR was determined by molecular replacement using the rat sfALR structure.    
  
   161 C was also determined to 2.9 A resolution by molecular replacement using the TbODC DFMO-bound structu
  
   163  alpha was determined at 2.3 A resolution by molecular replacement using the wild-type V alpha struct
   164 r has been determined to 2.1 A resolution by molecular replacement using truncated mouse ODC (Delta42
   165  2-phosphoglycolate (PGL), was determined by molecular replacement using X-ray diffraction data to 2.
   166 bitor (K(d) = 0.4 microM) were determined by molecular replacement using X-ray diffraction data to 2.
  
  
   169 ly, ResQ B-factor profile was used to assist molecular replacement, which resulted in successful solu
   170 9-9.0 A) was analyzed using a combination of molecular replacement with an energy-minimized model and
   171 AD+(gamma) was solved to 2.7 A resolution by molecular replacement with human class I beta1 beta1 ADH
  
  
   174 merization site, and its structure solved by molecular replacement with the model of fragment D.     
  
  
  
   178  that has been solved to 3.1 A resolution by molecular replacement with the structure of a dual funct
  
   180 vative of the native protein, and then using molecular replacement with the unrefined structure as a 
   181 ns that reach the high accuracy required for molecular replacement without any experimental phase inf
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