I find it amusing that you're willing to pay for multiple WoW accounts, but not for multiboxing software. Isn't that illegal?It's complicated.If you break any rules with 3rd party scripts then it was probably on purpose. There are useful functions that simply translate key-presses, such as making space right click or having custom spell modifiers; replicating key presses amongst multiple clients, as a mulit-boxer would, is also allowed.
Delays, sequences, automation, nesting, looping, etc are all disallowed. Although honestly they're almost impossible to detect.
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With the 5MP front camera, you can capture selfies that bring out your very best. On 22 November 2017 I dont recommend because of its weak battery from the first day of use, relatively unreal internal memory as I noticed there is no significant difference in the number of application capacity compared with my previous smart phone with only 8G internal memory What's good about this product: Thin, 4G, High resolution screen and compatible with many chargers What's not so good about this product: Weak, Non-removable battery and relatively unreal size of the internal memory.
Biochemical characterization of bovine RNAPII and RNAPII(G) After receiving the native bovine RNAPII and RNAPII(G) in ammonium-sulphate precipitant, the proteins were thawed and exchanged into physiological buffer conditions. At that stage, the RNAPII and RNAPII(G) enzymes were examined for their subunit composition on a SDS–PAGE stained by Coomassie Blue. As shown in, the Gdown1 in the native RNAPII(G) appears to be approximately stoichiometric when compared with the two largest RNAPII subunits, with the ratio Rpb1: Rpb2: Gdown1∼0.81: 1: 0.74.
Both forms of polymerase were tested for their activity in a nonspecific transcription elongation assay with tailed DNA template without the requirement of general transcription initiation factors. RNAPII and RNAPII(G) were active in generating early arrested RNA transcripts of 13–16 bases length and additional readthrough products of various lengths. Quantitation of early arrest or readthrough transcripts indicated a 1.5- to 2.5-fold increase in the amount of transcripts by RNAPII(G) compared with those of RNAPII. This increase in activity of RNAPII(G) compared with RNAPII was also observed by others (; ). We further analysed Gdown1's propensity as a disordered protein by rendering its sequence to folding analysis. Interestingly, the major folded region of Gdown1 appears to be in the N-terminal half, ranging from amino acid 55–113. To validate such prediction, recombinant Gdown1 proteins were subjected to limited trypsin proteolysis followed by mass spectroscopy.
As anticipated, the cleavage mainly took place in the C-terminal region. Biochemical and bioinformatics characterization of RNAPII(G).
( A) Purification of native RNAPII and RNAPII(G). Both forms of calf thymus RNAPII are presented in the SDS–PAGE Coomassie stained gel, with Gdown1 and the RNAPII subunits Rpb1, Rpb2, and Rpb3 labelled. By dividing the integrated intensity over the respective molecular weight, the relative amounts of Rpb1, Rpb2, and Gdown1 in RNAPII(G) were determined to be 0.81: 1: 0.74. ( B) Nonspecific transcription elongation assays.
0.4 and 0.8 μg of RNAPII (lanes 1–2) and RNAPII(G) (lanes 4–5) were used for the assays as previously described. RNA fragments from the early arrest or read-through are marked. As a control, α-amanitin, an RNAPII inhibitor, was added to RNAPII (lane 3) and RNAPII(G) (lane 6), respectively. All six lanes were from the same blot and only irrelevant lanes have been removed for the figure. Lanes 1 and 2 correspond to lanes 1 and 2 in the source gel; lane 3 corresponds to lane 4 in the source gel and lanes 4–6 correspond to lanes 6–8 in the source gel. The source data has been uploaded for full information.
( C) Folding analysis of Gdown1. Program FoldIndex was used to evaluate the folding propensity of Gdown1. Two folded domains found are marked in green and unfolded region in red. ( D) Limited proteolysis assay performed with trypsin.
Single letter amino acid codes in the predicted folded region are denoted in green in contrast to the red colour for those in the predicted unfolded region. Cleavage sites of peptide fragments identified by mass spectrometry are labelled by blue carets while protected protease sites are denoted by black carets. Figure source data can be found with the. Image analyses of native bovine RNAPII complexes. ( A) Native bovine RNAPII(G), enriched in monomers (white circles), were preserved in negative stain (2% uranyl acetate, 50 nm bar scale). ( B) Upper row: class averages of bovine RNAPII(G) particles obtained after reference-free alignment and clustering reveal renowned RNAPII features such as groove and stalk (Rpb4/7). Lower row: re-projections from the 3D reconstruction of native RNAPII(G) that best match the class averages above.
( C) EM structure of the native bovine RNAPII(G) superimposed with the yeast RNAPII X-ray structure (PDB: 1WCM). ( D) Native bovine RNAPII, enriched in dimers (white circles), preserved in negative stain (50 nm scale bar scale). ( E) A representative class average of RNAPII dimer. ( F) 3D model of the RNAPII dimer built from reconstruction RNAPII monomers. An orientation best matches the class average in ( E) shows subunit Rpb3 and Rpb4 likely participate the dimer interface.
Gdown1 blocks the interaction between RNAPII and TFIIF To confirm that Gdown1 impedes TFIIF association with RNAPII, competition assays using size exclusion chromatography, namely gel filtration, were employed. To assess the migration behaviour of RNAPII, RNAP–TFIIF and TFIIF on a gel-filtration column, excess amount of recombinant human TFIIF (16 μg) were incubated with bovine RNAPII (10 μg, RNAPII to TFIIF ratio 1:8) and subjected to fractionation. As shown in, the silver-stained SDS–PAGE gel reveals the four largest subunits of RNAPII (Rpb1–Rpb3, Rpb5) and two subunits of TFIIF (RAP74 and RAP30), allowing for assignment of the molecular constituent in each fraction. Following these bands as markers, it appeared that RNAPII spread across many fractions (fractions 19–29). Nevertheless, RNAPII peaked in earlier fractions (fractions 20–22) together with the seemingly stoichiometric TFIIF co-migrating, indicating that the constituent was the RNAPII–TFIIF complex. The excess amount of free TFIIF (fractions 24–35) was partially resolved from the RNAPII–TFIIF complex (fractions 20–22) and ran slightly behind as anticipated.
Likewise, an excess of Gdown1 (4 μg) was added to RNAPII (10 μg, RNAPII to Gdown1 ratio 1:4) to form the RNAPII–Gdown1 complex, resulting in a similar gel-filtration pattern; the RNAPII–Gdown1 complex appeared earlier (fractions 20–23) and the free Gdown1 followed (fractions 26–28). Interestingly, as Gdown1 was added to the pre-formed RNAPII–TFIIF complex, the TFIIF bands used to co-migrate with RNAPII in those earlier fractions (fractions 20–22) were retarded to the major positions of free TFIIF (after fraction 24). The replacement of TFIIF by Gdown1 in those earlier fractions indicates that Gdown1 displaces TFIIF from RNAPII, in keeping with the proposed steric exclusion mechanism.
On the contrary, in the reverse experiment, the excess TFIIF (16 μg) employed to challenge the pre-formed RNAPII–Gdown1 failed to displace Gdown1 bound to RNAPII. Competition assay using fractionation on a size exclusion column (Superose 6). ( A) Major fractions of RNAPII–TFIIF complex (18–22) and major fractions of excess amount of free TFIIF (24–35) are visualized on SDS–PAGE with silver staining. To form RNAPII–TFIIF, eight-fold TFIIF was used. ( B) Fractions of RNAPII–Gdown1 complex (20–23) and major fractions of free Gdown1 (26–28). To form RNAPII–Gdown1, four-fold Gdown1 was used ( C) The RNAII–TFIIF complex challenged by Gdown1.
The RNAPII-associated TFIIF (18–22) now disengages and becomes mostly free (24–35). RNAPII bound TFIIF are replaced by Gdown1 (19–22).
( D) The RNAPII–Gdown1 complex challenged by TFIIF. Gdown1 remains mostly associated with RNAPII (21–24) and TFIIF remains free (25–35). Marked bands are major RNAPII subunits: Rpb1 (220 kDa), Rpb2 (133 kDa), Rpb3 (31 kDa), Rpb5 (25 kDa), TFIIF subunits: RAP74 (74 kDa), RAP30 (28 kDa), and rGdown1. In the gel, M stands for marker and L for load. The stained gel strip on the left of each panel represents ∼2.5% of the column load. Discussion In this study, the single-particle cryo-EM technique was used to visualize the 3D structure of mammalian RNAPII and its isoform RNAPII(G) in the unstained state. Importantly, the Gdown1 domain ‘a' of ∼6 kDa was found situated on the Rpb5 shelf and connected to the adjacent Rpb1 jaw.
It is noted that the interactions between Gdown1 and RNAPII in this region was recently reported by using cross-linking method. Our observation of Gdown1 on RNAPII supports the idea that it is largely flexible or disordered because otherwise a bulky volume as large as the stalk of Rpb4–Rpb7 (45 kDa) would have been detected. Although at the current resolution, it is difficult to define the domain organization or orientation of Gdown1 on RNAPII, some questions along this line can be addressed: for instance, what would be the primary sequence that corresponds to Gdown1-a domain that seems to have a good tertiary structure? This sequence has to meet two criteria: (1) domain criterion; it forms a fold that resists proteolysis; (2) proximity criterion; it is close to the N-terminus because Gdown1-a is near the antibody recognizing the GST fused to the N-terminus (. Steric model of Gdown1 repression and relief by Mediator. In this model, Mediator acts as a scaffold to promote the association of RNAPII with TFIIF to create an unfavourable circumstance for Gdown1 to dwell on RNAPII at the overlapping sites of TFIIF; henceforth destabilizing the association between RNAPII and Gdown1 and eventually yielding the swapping between Gdown1 and TFIIF on RNAPII to allow for transcription initiation to ensue (RNAPII is coloured in cyan, Gdown1 in green, TFIIF in blue, and Mediator in grey.
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PIC stands for ‘pre-initiation complex'). ( A) When RNAPII(G) is recruited to the promoter, the PIC would not be generated considering the exclusion of TFIIF on RNAPII and transcription would be prevented. ( B) Steric hindrance of TFIIF binding to RNAPII by Gdown1 is relieved by the Mediator complex and Mediator swaps TFIIF for Gdown1 on RNAPII. ( C) Once Gdown1 is removed, promoter escape ensues with the possibility of some RNAPII enzymes to re-associate with Gdown1, in accord with recent findings of RNAPII(G) downstream of promoters and others to remain with TFIIF. Considering that RNAPII(G) is substoichiometric, it is also possible that RNAPII initiates at promoters in the absence of Gdown1 and therefore unhindered by Gdown1. At the level of elongation, one would ask what and how Gdown1 might do since Gdown1 would take place of TFIIF, which is thought to remain associated with RNAPII after the promoter clearance and drastically increase the rate of transcription (; ).
First, the regulatory effect through steric interference by Gdown1 may not be limited to TFIIF but can be applicable to a number of RNAPII-associated elongation proteins other than TFIIF. For example, it is known that stalling of RNAPII can occur near the promoter, which depends on proteins of DSIF and NELF (, ). Such promoter proximal pausing is relieved by pTEFb phosphorylating Rpb1, the largest RNAPII subunit. Can Gdown1 interfere with the binding of DSIF? To examine such, we compared our RNAPII–Gdown1 structure with the related one in which the RNAP is associated with Spt5, the homologue of DSIF , and also with the structure of RNAPII–TFIIS or RNAPII–CE , and therefore suggested that Gdown1 would affect DSIF but would not do so to TFIIS or CE.
These conjectures have been confirmed by Price's in-vitro experiments. Secondly, the observation of modest 1.5- to 2.5-fold increase in RNA production and the transcript length enhancement by Gdown1 , though less efficient than TFIIF, prompts us to suspect that Gdown1 is a RNAPII processivity factor. Perhaps our EM structures presented herein would account for the structural basis of the enhancement of elongation and that the common enhancement of Gdown1 and TFIIF may be the result of their association with the common RNAPII regions by stabilizing the elongation prone conformation of RNAPII and restraining template release. To elaborate, consider that Gdown1-a on the Rpb1 Jaw-Rpb5 shelf can contribute to securing the incoming DNA and the C-terminal region has potential cryptic DNA-binding activity for upstream DNA (; ), while the entirety of Gdown1 can impact the relative positions and/or stability of the two RNAPII mobile elements: the jaw lobe and the clamp. By encompassing the DNA on all sides, akin to closing a door, which is slightly ajar, the opportunity for DNA to depart from the enzyme is greatly reduced. That Gdown1 can work as a processivity factor is in accordant with the observation of RNAPII elongation complexes entering productive elongation without loss of Gdown1.
Considering that a Gdown1 homologue does not exist in yeast, the question as to Gdown1's role in metazoans is raised. Perhaps for complex organism development there is much that can go wrong and Gdown1 presents an additional level of scrutiny requiring careful execution of gene expression. We also speculate that Gdown1 may be a master brake, limiting unwanted transcription of some genes by preferentially localized with proximity to their promoters (; ) until Mediator removes Gdown1 and allows for TFIIF association. Another important need for Gdown1 could be in processivity, especially for extremely long genes such as the 2.5-Mb human dystophin gene which can require 16 h to transcribe.
Gdown1 would secure and stabilize the elongation complex, yet be compatible with the TFIIS elongation factor to aid in generating complete RNA transcripts. Such large genes are mostly metazoan specific, which perhaps explains a need for Gdown1 in higher organisms to generate some very extended RNA molecules. In conclusion, our study has revealed a structural basis underlying the Gdown1 regulatory mechanism in part by restricting TFIIF association with RNAPII. In general, it is suggested that Gdown1 can restrict or permit RNAPII-binding proteins other than TFIIF that are involved in initiation and elongation.
RNAPII and RNAPII(G) purification RNAPII and RNAPII (G) were purified as previously described. Briefly, RNAPII was enriched by precipitating the homogenized and clarified calf thymus extract with polyethyleneimine (PEI); the pellet was dissolved, cleared by centrifugation, followed by Mono Q chromatography, and affinity chromatography using a monoclonal 8WG16 antibody column.
Dual Boxing Programs L225
The eluted proteins were subjected to UNO-Q HPLC chromatography (Bio-Rad) to separate RNAPII and RNAPII(G). Both forms of RNAPII were stored as ammonium-sulphate precipitate under −80°C and shipped on dry ice via TNT service. For the subsequent EM and biochemical characterization, the frozen ammonium-sulphate precipitant was thawed immediately upon arrival, and dissolved in a buffer containing 50 mM Tris–Cl (pH=7.5), 200 mM potassium acetate (KOAc), 5 mM MgCl 2, 5 mM DDT and 10% glycerol. The removal of ammonium-sulphate was achieved by buffer exchange with the dissolving buffer using an Amicon centrifugal filter unit (MWCO 100 kDa; Millipore).
The proteins were further stored as aliquots (1 mg/ml) at −80°C. RNAPII(G) nonspecific promoter assay The transcription elongation assays were performed as previously described. Briefly, nonspecific initiation on a tailed template was employed.
The tailed template was formed by annealing a nontemplate strand: 5′-AACACCAGCGAGCAAGGCGTTTCGGGGAAGAAAAA, and a template strand: TTTTTCTTCCCCGAAACGCCTTGCTCGCTGGTGTTCCCCCCCCCCCC. 0.4 or 0.8 μg of polymerase, RNAPII or RNAPII(G), were employed, and α-amanitin, an RNAPII-specific inhibitor, was used as negative control. Quantification of bands was performed using the NIH free ImageJ software. Expression of recombinant human Gdown1 and TFIIF Recombinant Gdown1 expression plasmid, originally constructed in the pET151 vector , was subcloned into a pET21a vector using NdeI and NotI restriction sites. The Gdown1 protein was overexpressed in BL21 cells (Invitrogen) by IPTG induction (0.4 mM) and grown overnight at 20°C.
The protein was purified by using a nickel-NTA column with standard procedure as described by the manufacturer (Sigma). Further HPLC purification was depicted in.
The purified proteins were stored at −80°C. A bacterial expression plasmid encoding human TFIIF was constructed in the pACYCduet1 vector. To express TFIIF, Escherichia coli BL21 (DE3)-RIL cells (Merck) transformed with the TFIIF containing duet plasmid was grown at 37°C and the temperature was lowered to 30°C when OD reached 0.4 for induction with 0.84 mM IPTG. The cells were further grown for 3 h at 30°C before harvest.
TFIIF was purified using a nickel-NTA column in the same manner as Gdown1 was, with slight modifications in the washing step by raising the concentration of NaCl to 300 mM and that of imidazole to 40 mM (see also ). Size exclusion chromatography assays To form RNAPII–Gdown1 or RNAPII–TFIIF complex, 10 μg of bovine RNAPII was mixed with individual recombinant proteins, rGdown1 or rTFIIF, and incubated for 60 min at 20°C, respectively. For rGdown1, 4 μg was used, representing a rGdown1 to RNAPII ratio of 4:1. As to the formation of RNAPII–TFIIF, about eight-fold recombinant TFIIF (16 μg) was used. The size exclusion chromatography was carried out using the AKTA purifier system (GE Health/Amersham Biosciences). A Superose 6 column PC 3.2/30 (GE Healthcare) was equilibrated with equilibrating buffer (50 mM Tris–HCl (pH 7.5 at 4°C), 100 mM NaCl, 1 mM TCEP, and 1% protease inhibitor cocktail). The protein sample (∼30 μl) was loaded onto the column for fractionation with a total elution volume of 3.2 ml at a flow rate of 0.06 ml/min.
The fractions were collected with 60 μl per fraction. The protein complex in each fraction was concentrated with nickel beads (Sepharose High Performance, GE Healthcare). In brief, 10 μl pre-equilibrated Ni-beads were added to individual fraction from (15–35) respectively, and incubated with mixing at 4°C overnight. The supernatant was discarded; the same volume of 2 × SDS–PAGE sample buffer was added to the beads, boiled on a heating block for 10 min.
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The denatured protein samples were separated on a NuPAGE 4–12% Bis-Tris gel using MES running buffer and visualized with silver stain. In all, 5 μl of 10-fold diluted protein ladder was loaded onto an SDS–PAGE gel. To challenge RNAPII–Gdown1 with rTFIIF, RNAPII was first incubated with four-fold rGdown1 at 20°C and mixed at 550 r.p.m. After the first incubation period, eight-fold rTFIIF was added, and another 60 min of incubation was performed, followed by loading the protein samples onto a Superpose 6 PC 3.2/30 size exclusion column. To challenge RNAPII–TFIIF with rGdown1, RNAPII was first incubated with four-fold rGdown1, and eight-fold rTFIIF was added after the first incubation period for an additional incubation period before size exclusion chromatography was carried out. EM sample preparation In brief, a frozen aliquot of bovine RNAPII or RNAPII(G) (1 mg/ml) was freshly thawed and diluted with de-ionized water to a final concentration of 50 μg/ml for direct EM usage or for reconstitution.
To reconstitute bovine RNAPII complexes, incubation of bovine RNAPII with additional proteins were performed at 20°C for 60 min before the EM sample was prepared. To form a RNAPII–Gdown1 complex, the molar ratio of recombinant Gdown1 to RNAPII was adjusted to 4:1. For RNAPII–elongation complexes, three-fold of nucleic acid scaffold containing the bubble DNA and a 35-nt RNA was used. For RNAPII–TFIIF, six-fold recombinant TFIIF together with three-fold nucleic acid scaffold was added. In this study, three different techniques for preserving RNAPII complexes were employed, including negative-stain, cryo-staining and unstained cryo. To make an EM specimen, 3 μl of protein solution was applied to Cu grid (300 mesh) or quantifoil grid coated with thin carbon film to enhance the Thon ring observation. The carbon film was made by evaporating a carbon rod onto a cleaved mica sheet with an evaporator (Edwards Auto 306), deposited on the grid to dry, and freshly discharged with amylamine in a glow-discharger (EM Science, EM-100) before applying protein solution.
For the negative-stain technique, 2% uranyl acetate was used; the sample was either sandwiched by another layer of thin carbon or deep-stained. For cryo-staining, the protein-adsorbed grids were first stained with 1% uranyl acetate and not allowed to dry; the sample was immediately blotted with a filter paper (Wattmann No.
1, smooth side) and plunged into liquid ethane with a customer built plunger in a cold room with 80% humidity (; ). The frozen EM samples were then stored under liquid nitrogen before EM. For unstained cryo preservation, the procedure was the same as cryo-staining except no staining agent was used. Immuno-electron microscopy For antibody decoration against the GST-tagged Gdown1 in the RNAPII–Gdown1 complex or against the RAP74 subunit within the RNAPII–TFIIF complex, RNAPII complexes were incubated with two-fold antibody and then subjected to gel filtration for fractionating the RNAPII–Gdown1 antibody or the RNAPII–TFIIF antibody complex. Application of the polyclonal antibody against Gdown1 also followed the same procedure. To disclose the location of the antibody in complex, a 120-kV TEM (JEOL 1400, LaB 6 filament, Cs=3.4 mm) and 4K × 4K CCD camera (Gatan 895) were used; the magnification used for visualizing antibody was × 104 000 and the defocus was∼1.5 μm.
We acknowledge the Instrument Center of Academia Sinica (AS), Institute of Chemistry of AS, and YK. Hwu at Institute of Physics of AS for cryo-electron microscopes. W-HC thanks Yao-Yin Chuang and Yi-Yum Chen for assistance on TEM, Chen-Yu Li for helping trypsin digestion and Ting-Yi Wu for boxing cryo-EM images, and the Mass Spectroscopy Center at Institute of Chemistry of AS. W-HC is grateful for Dr Burton for TFIIF plasmids.
W-HC and AG are indebted to Dr Price for anti-Gdown1 antibody and to Dr Price and Dr Roeder for communicating unpublished results of Gdown1. W-HC was supported by AS Thematic Grant (AS-99-TP-A03), AS Nanoscience programme, and National Science Council (NSC) of Taiwan (NSC99-2113-M-001-022-MY3 and NSC98-2113-M-001-020) for this work; Dr Y-M Wu and Y-C Lin have been supported by NSC postdoctoral fellowships (NSC98-2811-M-001-141, NSC96-2811-M-001-083 respectively). XH was supported by Natural Science Foundation of China (Nos. AG was supported by the National Institutes of Health Grant (GM64474) and by the DOD Breast Cancer IDEA Award BC083495. Author contributions: YM Wu did cryo-EM and image reconstruction; JW Chang did gel-filtration competition assays; JW Chang, SH Huang, and PL Wu did antibody EM; YC Lin compiled reconstruction algorithm; CH Wang and CC Chang did GST fusion and subcloning of recombinant TFIIF and Gdown1; X Hu did pull-down assay; X Hu and A Gnatt purified RNAPII and RNAPII(G).
YM Wu and WH Chang designed the experiments and analysed the data; YM Wu, JW Chang, X Hu, A Gnatt, and WH Chang wrote the manuscript. Results and opinions herein represent those of the authors alone and not of the funding institutions unless otherwise specified.
Won't get me banned.:-)That part is less dependent on the specific software you use and more dependent on how you use it. The features that allow multicasting software to work are intrinsically capable of violating Blizzard's automation clauses. It is your responsibility to know those clauses and not use the software in ways that violate those clauses.
However, most of the informational sites about multi-boxing will tell you what not to do. The important guidelines are: If you issue one keypress/mouseclick, each game client receives no more than one keypress/mouseclick. Modifying a keypress (setting up a button to issue a shift+f1 event on a single keypress, for example) is acceptable; but sending sequential kepresses/clicks is not. The distinction has to do with what specifically constitutes single/multiple hardware events (modifier keys are not considered discrete hardware events in this context). You are also not allowed to set your software up to issue any hardware events without you issuing an actual hardware event (you cannot set it to press a button every 5 minutes to keep you from logging out, for example), whether or not you are triggering a protected function with that event. This is because requiring a hardware event is oen of Blizzard's methods for preventing automation of certain functions (spellcasting, targeting, movement, posting auctions, etc.).
If you cannot automate it with an addon or macro; do not use your multiboxing software to automate it and you will be fine. 11:51 PMPosted by I wonder how people find threads like this and make this the only post in their posting history. There is a inverse correlation between posting comments and necro-ing old threads. But, while I'm here I might as well give my two cents. I leveled almost 25 characters to 80 using RaF on a macbook air without any dual boxing software installed at all.
I just created two shortcuts, one to the wow.exe file and another to the launcher. I would run both programs and command+tab (alt+tab for windows) between the two. I even got so good at doing this that I could heal an entire dungeon group (getting compliments several times on how good my healing was) and also out dps 1 or 2 of the people in my group at the same time. It doesn't take any fancy software to dual box and I would recommend anyone try it because it cuts leveling time by an insane amount.
It took me less than one month to get an entire realm full of 80's by following the pattern of leveling a pair of 80's and then leveling another set to 41 to grant the remaining 39 levels. My average leveling time to 80 was 24 hours of /played time and it took me around 8 hours to get to level 41. The best part of this? Wotlk is essentially free if you buy the battle chest (which is marked down to $10 now) and I bought it during the Christmas special, so the grand total I paid for all these level 80's was $5. Just my two cents.
Thank you for all of the helpful tips and hints on dual boxing. All y'alls advise really helped me. I recently did the RAF option and I'm currently just dual Boxing using the helium addon and macros which remarkably work well. I have already finished leveling a disc priest and tank druid to level 69 as heals and tank while running dungeons. I read a post some where how some one did tank and heals while dungeon running and it intrigued me, so i thought I'd try it. It is very fun and I leveled the 2 toons to 69 in roughly 3 days of casual game time play. I have noticed though since I've started a different combo that the monk class is superb for tanking while dual boxing, however druid heals in combination is more challenging than when I was using my disc priest.
Not sure if any of y'all run macro dual box tank heals. FYI if your running macro's and dual boxing heals and tank, you'll probably cap out near lvl 69 as the Northrend dungeons require more independent actions that make it more difficult to run both heals and tank. Let me know if yall have any other advise as to good boxing methods.
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